Glycoside Hydrolase Family 29 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:19:20Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Harry Brumer: /* Three-dimensional structures */

2020-01-07T16:58:01Z

Three-dimensional structures

Harry Brumer: /* Three-dimensional structures */

2020-01-07T16:57:32Z

Three-dimensional structures

Harry Brumer: /* Three-dimensional structures */

2020-01-07T16:57:12Z

Three-dimensional structures

Harry Brumer at 16:53, 7 January 2020

2020-01-07T16:53:51Z

Harry Brumer: updated Clan entry in table

2020-01-07T16:52:02Z

updated Clan entry in table

Spencer Williams: /* Kinetics and Mechanism */

2013-06-27T05:48:30Z

Kinetics and Mechanism

Harry Brumer: /* References */

2013-05-10T16:02:55Z

References

Harry Brumer: updated CAZyDBlink

2012-05-11T16:57:20Z

updated CAZyDBlink

Spencer Williams at 11:45, 5 July 2010

2010-07-05T11:45:46Z

@@ Line 1: / Line 1: @@
 {{CuratorApproved}}
-* [[Author]]: ^^^Gerlind Sulzenbacher^^^
+* [[Author]]: [[User:Gerlind Sulzenbacher|Gerlind Sulzenbacher]]
-* [[Responsible Curator]]:  ^^^Steve Withers^^^
+* [[Responsible Curator]]:  [[User:Steve Withers|Steve Withers]]
 ----

@@ Line 43: / Line 43: @@
 The first crystal structure to be solved is that of the α-L-fucosidase from ''T. maritima'', Tmα-fuc (PDB ID [{{PDBlink}}1hl8 1hl8]). The simultaneous solution of the structures of an enzyme-product complex (PDB ID [{{PDBlink}}1odu 1odu]) and of a glycosyl-enzyme [[intermediate]] (PDB ID [{{PDBlink}}1hl9 1hl9]) allowed the unambiguous identification of the [[general acid/base]] <cite>8</cite>, as described above. Tmα-fuc assembles as a hexamer and displays a two-domain fold, composed of a catalytic (β/α)<sub>8</sub>-like domain and a C-terminal β-sandwich domain. The two key active site residues are located at the C-terminal ends of strands β-strands 4 (nucleophile) and 6 (acid/base).
 Crystallization experiments for the ''S. solfataricus'' α-L-fucosidase, Ssα-fuc, were not very fruitful, but a small angle scattering study has been reported <cite>11</cite>, which suggests a nonameric assembly of the enzyme in solution. Two crystal structures, arising from Structural Genomics initiatives, have been deposited in the [http://www.pdb.org/ Protein Data Bank] for α-L-fucosidases from ''Bacteroides thetaiotaomicron VPI-5482'', with accession numbers [{{PDBlink}}3eyp 3eyp] and [{{PDBlink}}3gza 3gza].
-The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in [[GH107]], which together with GH29 forms Clan GH-R. GH29 also bears some structural similarity to families [[GH13]] ([[Clan]] GH-H) and [[GH27]] ([[Clan]] GH-D).
+The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in [[GH107]], which together with GH29 forms [[Clan]] GH-R. GH29 also bears some structural similarity to families [[GH13]] ([[Clan]] GH-H) and [[GH27]] ([[Clan]] GH-D).
 == Transglycosylation and Glycosynthases ==

@@ Line 43: / Line 43: @@
 The first crystal structure to be solved is that of the α-L-fucosidase from ''T. maritima'', Tmα-fuc (PDB ID [{{PDBlink}}1hl8 1hl8]). The simultaneous solution of the structures of an enzyme-product complex (PDB ID [{{PDBlink}}1odu 1odu]) and of a glycosyl-enzyme [[intermediate]] (PDB ID [{{PDBlink}}1hl9 1hl9]) allowed the unambiguous identification of the [[general acid/base]] <cite>8</cite>, as described above. Tmα-fuc assembles as a hexamer and displays a two-domain fold, composed of a catalytic (β/α)<sub>8</sub>-like domain and a C-terminal β-sandwich domain. The two key active site residues are located at the C-terminal ends of strands β-strands 4 (nucleophile) and 6 (acid/base).
 Crystallization experiments for the ''S. solfataricus'' α-L-fucosidase, Ssα-fuc, were not very fruitful, but a small angle scattering study has been reported <cite>11</cite>, which suggests a nonameric assembly of the enzyme in solution. Two crystal structures, arising from Structural Genomics initiatives, have been deposited in the [http://www.pdb.org/ Protein Data Bank] for α-L-fucosidases from ''Bacteroides thetaiotaomicron VPI-5482'', with accession numbers [{{PDBlink}}3eyp 3eyp] and [{{PDBlink}}3gza 3gza].
-The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in [[GH107]], which together with GH29 forms Clan GH-R. GH29 also bears some structural similarity to families [[GH13]] (Clan GH-H) and [[GH27]] (Clan GH-D).
+The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in [[GH107]], which together with GH29 forms Clan GH-R. GH29 also bears some structural similarity to families [[GH13]] ([[Clan]] GH-H) and [[GH27]] ([[Clan]] GH-D).
 == Transglycosylation and Glycosynthases ==

@@ Line 43: / Line 43: @@
 The first crystal structure to be solved is that of the α-L-fucosidase from ''T. maritima'', Tmα-fuc (PDB ID [{{PDBlink}}1hl8 1hl8]). The simultaneous solution of the structures of an enzyme-product complex (PDB ID [{{PDBlink}}1odu 1odu]) and of a glycosyl-enzyme [[intermediate]] (PDB ID [{{PDBlink}}1hl9 1hl9]) allowed the unambiguous identification of the [[general acid/base]] <cite>8</cite>, as described above. Tmα-fuc assembles as a hexamer and displays a two-domain fold, composed of a catalytic (β/α)<sub>8</sub>-like domain and a C-terminal β-sandwich domain. The two key active site residues are located at the C-terminal ends of strands β-strands 4 (nucleophile) and 6 (acid/base).
 Crystallization experiments for the ''S. solfataricus'' α-L-fucosidase, Ssα-fuc, were not very fruitful, but a small angle scattering study has been reported <cite>11</cite>, which suggests a nonameric assembly of the enzyme in solution. Two crystal structures, arising from Structural Genomics initiatives, have been deposited in the [http://www.pdb.org/ Protein Data Bank] for α-L-fucosidases from ''Bacteroides thetaiotaomicron VPI-5482'', with accession numbers [{{PDBlink}}3eyp 3eyp] and [{{PDBlink}}3gza 3gza].
-The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in families [[GH13]] and [[GH27]].
+The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in [[GH107]], which together with GH29 forms Clan GH-R. GH29 also bears some structural similarity to families [[GH13]] (Clan GH-H) and [[GH27]] (Clan GH-D).
 == Transglycosylation and Glycosynthases ==

@@ Line 41: / Line 41: @@
 == Three-dimensional structures ==
-Very few structures are available for GH29 enzymes. The first crystal structure to be solved is that of the α-L-fucosidase from ''T. maritima'', Tmα-fuc (PDB ID [{{PDBlink}}1hl8 1hl8]). The simultaneous solution of the structures of an enzyme-product complex (PDB ID [{{PDBlink}}1odu 1odu]) and of a glycosyl-enzyme [[intermediate]] (PDB ID [{{PDBlink}}1hl9 1hl9]) allowed the unambiguous identification of the [[general acid/base]] <cite>8</cite>, as described above. Tmα-fuc assembles as a hexamer and displays a two-domain fold, composed of a catalytic (β/α)<sub>8</sub>-like domain and a C-terminal β-sandwich domain. The two key active site residues are located at the C-terminal ends of strands β-strands 4 (nucleophile) and 6 (acid/base).
+The first crystal structure to be solved is that of the α-L-fucosidase from ''T. maritima'', Tmα-fuc (PDB ID [{{PDBlink}}1hl8 1hl8]). The simultaneous solution of the structures of an enzyme-product complex (PDB ID [{{PDBlink}}1odu 1odu]) and of a glycosyl-enzyme [[intermediate]] (PDB ID [{{PDBlink}}1hl9 1hl9]) allowed the unambiguous identification of the [[general acid/base]] <cite>8</cite>, as described above. Tmα-fuc assembles as a hexamer and displays a two-domain fold, composed of a catalytic (β/α)<sub>8</sub>-like domain and a C-terminal β-sandwich domain. The two key active site residues are located at the C-terminal ends of strands β-strands 4 (nucleophile) and 6 (acid/base).
 Crystallization experiments for the ''S. solfataricus'' α-L-fucosidase, Ssα-fuc, were not very fruitful, but a small angle scattering study has been reported <cite>11</cite>, which suggests a nonameric assembly of the enzyme in solution. Two crystal structures, arising from Structural Genomics initiatives, have been deposited in the [http://www.pdb.org/ Protein Data Bank] for α-L-fucosidases from ''Bacteroides thetaiotaomicron VPI-5482'', with accession numbers [{{PDBlink}}3eyp 3eyp] and [{{PDBlink}}3gza 3gza].
 The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in families [[GH13]] and [[GH27]].

@@ Line 11: / Line 11: @@
 |-
 |'''Clan'''
-|none
+|GH-R
 |-
 |'''Mechanism'''

@@ Line 31: / Line 31: @@
 == Kinetics and Mechanism ==
-GH29 α-fucosidases  are [[retaining]] enzymes following a [[classical Koshland double-displacement mechanism]], as first proposed in 1987 for human liver α-fucosidase ''via'' burst kinetics experiments and  using methanol as an alternative glycone acceptor to produce methyl α-L-fucoside <cite>2</cite>. This has been further confirmed by <sup>1</sup>H NMR monitoring of the reaction catalyzed by an α-L-fucosidase from ''Thermus sp.'' <cite>3</cite>, and a α-L-fucosidase from the marine mollusc ''Pecten maximus'' <cite>4</cite>, as well as by COSY and <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the [[transglycosylation]] action of ''Sulfolobus solfataricus'' α-L-fucosidase, Ssα-fuc <cite>5</cite>. [[GH95]] α-fucosidases, in contrast, operate with inversion of the anomeric configuration.
+GH29 α-fucosidases  are [[retaining]] enzymes following a [[classical Koshland double-displacement mechanism]], as first proposed in 1987 for human liver α-fucosidase ''via'' burst kinetics experiments and  using methanol as an alternative glycone acceptor to produce methyl α-L-fucoside <cite>2</cite>. This has been further confirmed by <sup>1</sup>H NMR monitoring of the reaction catalyzed by an α-L-fucosidase from ''Thermus sp.'' <cite>3</cite>, and a α-L-fucosidase from the marine mollusc ''Pecten maximus'' <cite>4</cite>, as well as by COSY and <sup>1</sup>H-<sup>13</sup>C NMR spectroscopy analysis of the interglycosidic linkage of disaccharides formed by the [[transglycosylases|transglycosylase]] action of ''Sulfolobus solfataricus'' α-L-fucosidase, Ssα-fuc <cite>5</cite>. [[GH95]] α-fucosidases, in contrast, operate with inversion of the anomeric configuration.
 == Catalytic Residues ==

@@ Line 68: / Line 68: @@
 #11 pmid=15207718
 #12 pmid=17240986
-#13 Cobucci-Ponzano B, Conte F, Bedini E, Corsaro MM, Parrilli M, Sulzenbacher G, Lipski A, Dal Piaz F, Lepore L, Rossi M, and Moracci, M. ''β-glycosyl azides as substrates for α-glycosynthases: preparation of efficient α-L-fucosynthases''. Chem Biol 2009 Oct; 16(10) 1097-108. [http://linkinghub.elsevier.com/retrieve/pii/S1074552109003238 DOI: 10.1016/j.chembiol.2009.09.013]
+#13 pmid=19875083
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH029]]

@@ Line 21: / Line 21: @@
 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/fam/GH29.html
+| colspan="2" |{{CAZyDBlink}}GH29.html
 |}
 </div>

@@ Line 34: / Line 34: @@
 == Catalytic Residues ==
-The [[catalytic nucleophile]] in GH29 was first identified in the ''Sulfolobus solfataricus'' α-L-fucosidase, Ssα-fuc, as Asp242 in the sequence VYF<u>'''D'''</u>WWI via chemical rescue of an inactive mutant with sodium azide <cite>6</cite>. Concomitantly the [[catalytic nucleophile]] of ''Thermotoga maritima'' α-L-fucosidase, Tmα-fuc, was confirmed to be Asp224 in the sequence LWN<u>'''D'''</u>MGW through trapping of the 2-deoxy-2-fluorofucosyl-enzyme [[intermediate]] and subsequent peptide mapping via LC-MS/MS technologies, as well as by chemical rescue of an inactive mutant <cite>7</cite>. The trapping of the 2-deoxy-2-fluorofucosyl-enzyme intermediate in Tmα-fuc was corroborated by crystallographic studies <cite>8</cite>. The [[catalytic nucleophile]] of the human enzyme FucA1 has recently been identified as being Asp225 <cite>9</cite>.
+The [[catalytic nucleophile]] in GH29 was first identified in the ''Sulfolobus solfataricus'' α-L-fucosidase, Ssα-fuc, as Asp242 in the sequence VYF<u>'''D'''</u>WWI via chemical rescue of an inactive mutant with sodium azide <cite>6</cite>. Concomitantly the [[catalytic nucleophile]] of ''Thermotoga maritima'' α-L-fucosidase, Tmα-fuc, was confirmed to be Asp224 in the sequence LWN<u>'''D'''</u>MGW through trapping of the 2-deoxy-2-fluorofucosyl-enzyme [[intermediate]] and subsequent peptide mapping via LC-MS/MS technologies, as well as by chemical rescue of an inactive mutant <cite>7</cite>. The trapping of the 2-deoxy-2-fluorofucosyl-enzyme [[intermediate]] in Tmα-fuc was corroborated by crystallographic studies <cite>8</cite>. The [[catalytic nucleophile]] of the human enzyme FucA1 has recently been identified as being Asp225 <cite>9</cite>.
 Whereas the [[catalytic nucleophile]] in GH29 has been shown to be a conserved aspartate residue, the identity of the [[general acid/base]] is still controversial.  Structural and mutagenesis studies of Tmα-fuc provided strong evidence for the variant Glu266 being the [[general acid/base]] <cite>8</cite>. In the crystal structure the carboxyl function of this residue is 5.5 Å away from that of the [[catalytic nucleophile]] Asp224, a distance commonly observed in retaining glycosidases proceeding ''via'' a [[classical Koshland double-displacement mechanism]]. Although multiple sequence alignments show that Glu266 is not conserved within GH29, the residue is structurally conserved in two 3-D structures of α-L-fucosidases from ''Bacteroides thetaiotaomicron VPI-5482'', recently deposited in the [http://www.pdb.org/ Protein Data Bank] (PDB accession numbers [{{PDBlink}}3eyp 3eyp] and [{{PDBlink}}3gza 3gza]). Studies of Ssα-fuc demonstrated that mutation of the Glu residue corresponding in sequence to Tmα-fuc Glu266 barely impaired the catalytic activity of the enzyme, whereas a Glu58Gly mutant had a 4000 fold lower ''k<sub>cat</sub>/K<sub>M</sub>'' and could be chemically rescued <cite>10</cite>. In the crystal structure of Tmα-fuc in complex with fucose <cite>8</cite>, the residue corresponding to Ssα-fuc Glu58, Glu66, is found 7.5 Å away from the [[catalytic nucleophile]] Asp224 and hydrogen bonded to the C-3 hydroxyl group of fucose, which altogether makes this residue an unlikely candidate for the function of the [[general acid/base]]. A recent study of the human α-L-fucosidase FucA1, carefully done combining bioinformatics, structural modelling, mutagenesis, chemical rescue with azide and <sup>1</sup>H NMR spectral analysis, identified Glu289 as the [[general acid/base]] <cite>9</cite>. The equivalent residue in Tmα-fuc, Glu281, as inferred from sequence alignment of FucA1 and Tmα-fuc, points to the interior of the (β/α)<sub>8</sub> barrel and lies about 15 Å apart form the catalytic centre.
@@ Line 41: / Line 41: @@
 == Three-dimensional structures ==
-Very few structures are available for GH29 enzymes. The first crystal structure to be solved is that of the α-L-fucosidase from ''T. maritima'', Tmα-fuc (PDB ID [{{PDBlink}}1hl8 1hl8]). The simultaneous solution of the structures of an enzyme-product complex (PDB ID [{{PDBlink}}1odu 1odu]) and of a glycosyl-enzyme intermediate (PDB ID [{{PDBlink}}1hl9 1hl9]) allowed the unambiguous identification of the [[general acid/base]] <cite>8</cite>, as described above. Tmα-fuc assembles as a hexamer and displays a two-domain fold, composed of a catalytic (β/α)<sub>8</sub>-like domain and a C-terminal β-sandwich domain. The two key active site residues are located at the C-terminal ends of strands β-strands 4 (nucleophile) and 6 (acid/base).
+Very few structures are available for GH29 enzymes. The first crystal structure to be solved is that of the α-L-fucosidase from ''T. maritima'', Tmα-fuc (PDB ID [{{PDBlink}}1hl8 1hl8]). The simultaneous solution of the structures of an enzyme-product complex (PDB ID [{{PDBlink}}1odu 1odu]) and of a glycosyl-enzyme [[intermediate]] (PDB ID [{{PDBlink}}1hl9 1hl9]) allowed the unambiguous identification of the [[general acid/base]] <cite>8</cite>, as described above. Tmα-fuc assembles as a hexamer and displays a two-domain fold, composed of a catalytic (β/α)<sub>8</sub>-like domain and a C-terminal β-sandwich domain. The two key active site residues are located at the C-terminal ends of strands β-strands 4 (nucleophile) and 6 (acid/base).
 Crystallization experiments for the ''S. solfataricus'' α-L-fucosidase, Ssα-fuc, were not very fruitful, but a small angle scattering study has been reported <cite>11</cite>, which suggests a nonameric assembly of the enzyme in solution. Two crystal structures, arising from Structural Genomics initiatives, have been deposited in the [http://www.pdb.org/ Protein Data Bank] for α-L-fucosidases from ''Bacteroides thetaiotaomicron VPI-5482'', with accession numbers [{{PDBlink}}3eyp 3eyp] and [{{PDBlink}}3gza 3gza].
 The catalytic domain of Tmα-fuc does not adopt the canonical TIM-barrel (β/α)<sub>8</sub> fold, as it lacks helices α5 and α6. Helix α5 is also missing in the structure of one of the ''B. thetaiotaomicron VPI-5482'' α-L-fucosidases, BT3798 (PDB ID [{{PDBlink}}3gza 3gza]), whereas α-L-fucosidase BT2192 (PDB ID [{{PDBlink}}3eyp 3eyp]) from the same organism adopts the canonical TIM-barrel fold. The three structures differ furthermore by the insertion/deletion of a considerable number of additional α-helices, 3<sub>10</sub> helices, and extended surface loop regions. The closest structural homologues of GH29 enzymes within the CAZy classification can be found in families [[GH13]] and [[GH27]].
@@ Line 52: / Line 52: @@
 ; First [[catalytic nucleophile]] identification : ''Sulfolobus solfataricus'' α-L-fucosidase by azide rescue of an inactivated mutant <cite>6</cite> and confirmed shortly thereafter by labeling of the nucleophile and peptide mapping <cite>7</cite>.
 ; First [[general acid/base]] residue identification : ''Thermotoga maritima'' α-fucosidase by X-ray structural analysis and mutagenesis <cite>8</cite>.
-; First 3-D structure : ''Thermotoga maritima'' α-fucosidase, free  enzyme ([{{PDBlink}}1hl8 PDB 1hl8]), product complex ([{{PDBlink}}1odu PDB 1odu]) and glycosyl-enzyme intermediate ([{{PDBlink}}1hl9 PDB 1hl9]) <cite>8</cite>.
+; First 3-D structure : ''Thermotoga maritima'' α-fucosidase, free  enzyme ([{{PDBlink}}1hl8 PDB 1hl8]), product complex ([{{PDBlink}}1odu PDB 1odu]) and glycosyl-enzyme [[intermediate]] ([{{PDBlink}}1hl9 PDB 1hl9]) <cite>8</cite>.
 == References ==