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Difference between revisions of "Carbohydrate Binding Module Family 71"

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== Ligand specificities ==
 
== Ligand specificities ==
Mention here all major natural ligand specificities that are found within a given family (also plant or mammalian origin). Certain linkages and promiscuity would also be mentioned here if biologically relevant.
+
The CBM family 71 was created in September 2014 with the characterization of the large multimodular b-galactosidase BgaA from Streptococcus pneumoniae(1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-b-1,4-D-glucose) and LacNAc (galactopyranosyl-b-1,4-N-acetyl-D-glucosamine).
 
 
''Note: Here is an example of how to insert references in the text, together with the "biblio" section below:'' Please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. CBMs, in particular, have been extensively reviewed <cite>Boraston2004 Hashimoto2006 Shoseyov2006 Guillen2010 Armenta2017</cite>.
 
  
 
== Structural Features ==
 
== Structural Features ==
''Content in this section should include, in paragraph form, a description of:''
+
The structure of CBM71-1 solved by X-ray crystallography shows a b-sandwich fold comprising opposing sheets of 4- and 5-antiparallel b-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both b-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).
* '''Fold:''' Structural fold (beta trefoil, beta sandwich, etc.)
 
* '''Type:''' Include here Type A, B, or C and properties
 
* '''Features of ligand binding:''' Describe CBM binding pocket location (Side or apex) important residues for binding (W, Y, F, subsites), interact with reducing end, non-reducing end, planar surface or within polysaccharide chains. Include examples pdb codes. Metal ion dependent. Etc.
 
 
 
 
== Functionalities ==  
 
== Functionalities ==  
''Content in this section should include, in paragraph form, a description of:''
+
The CBM71s are found as ancillary modules in the b-galactosidase BgaA from S. pneumoniae. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3)has been fully characterized in parallel with the characterization of CBM71s  (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).
* '''Functional role of CBM:''' Describe common functional roles such as targeting, disruptive, anchoring, proximity/position on substrate.
 
* '''Most Common Associated Modules:''' 1. Glycoside Hydrolase Activity; 2. Additional Associated Modules (other CBM, FNIII, cohesin, dockerins, expansins, etc.)
 
* '''Novel Applications:'''  Include here if CBM has been used to modify another enzyme, or if a CBM was used to label plant/mammalian tissues? Etc.
 
 
 
 
== Family Firsts ==
 
== Family Firsts ==
 
;First Identified
 
;First Identified
:Insert archetype here, possibly including ''very brief'' synopsis.
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The CBM71 modules were first identified through the characterization of the b-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.
 
;First Structural Characterization
 
;First Structural Characterization
:Insert archetype here, possibly including ''very brief'' synopsis.
+
The first crystal structures of family CBM71s were from the streptococcal b-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.  
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Cantarel2009 pmid=18838391
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#Singh2014 pmid=25210925
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
 
 
#Boraston2004 pmid=15214846
 
#Boraston2004 pmid=15214846
#Hashimoto2006 pmid=17131061
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#Cantarel209 pmid=18838391
#Shoseyov2006 pmid=16760304
 
#Guillen2010 pmid=19908036
 
#Armenta2017 pmid=28547780
 
 
</biblio>
 
</biblio>
  
 
[[Category:Carbohydrate Binding Module Families|CBM071]]
 
[[Category:Carbohydrate Binding Module Families|CBM071]]

Revision as of 13:41, 10 April 2019

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


CAZy DB link
http://www.cazy.org/CBM71.html

Ligand specificities

The CBM family 71 was created in September 2014 with the characterization of the large multimodular b-galactosidase BgaA from Streptococcus pneumoniae(1). Two CBMs, CBM71-1 (residues 1463-1645) and CBM71-2 (residues 1828-1998), were identified in the N-terminal region of this protein. The functional characterization of the CBMs reveals a binding specificity limited to lactose (galactopyranosyl-b-1,4-D-glucose) and LacNAc (galactopyranosyl-b-1,4-N-acetyl-D-glucosamine).

Structural Features

The structure of CBM71-1 solved by X-ray crystallography shows a b-sandwich fold comprising opposing sheets of 4- and 5-antiparallel b-strands and a bound structural metal ion modelled as a calcium (Figure 1). CBM71-1 structure in complex with LacNAc reveals a shallow binding site located at the apex of the b-fold opposite the N- and C-termini. The basis of CBM71-1 specificity for sugars with a terminal galactose resides in the W1514 side chain configuration, which provides CH-pinteractions with both b-linked pyranose rings of the disaccharide (Figure 2). CBM71-2, which possesses 35% sequence identity with CBM71-1, presents a very similar fold and an almost identical binding site. Therefore, the CBM71 family can be classified as type C CBM (2).

Functionalities

The CBM71s are found as ancillary modules in the b-galactosidase BgaA from S. pneumoniae. BgaA is a large multimodular cell surface exposed CAZyme comprising 17 modules of 7 different types. However, only the catalytic module belonging to the family 2 glycoside hydrolase (3)has been fully characterized in parallel with the characterization of CBM71s (1). In addition to their classical CBM role of focusing the enzyme to its substrate, the streptococcal CBM71s have been shown to contribute to pneumococcal adherence by binding lactose- and LacNAc-containing cell surface glycoconjugates (1).

Family Firsts

First Identified

The CBM71 modules were first identified through the characterization of the b-galactosidase BgaA from S. pneumoniae(1). CBM71-1 and CBM71-2 are the founding, and only characterized, members of the family.

First Structural Characterization

The first crystal structures of family CBM71s were from the streptococcal b-galactosidase BgaA (1). The crystallographic structures of a seleno-methionine derivative of CBM71-1 (PDB ID 4CUA), CBM71-1 in complex with LacNAc (PDB ID 4CUB) and CBM71-2 (PDB ID 4CU9) were deposited in the Protein Data Bank in September 2014.

References

  1. Singh AK, Pluvinage B, Higgins MA, Dalia AB, Woodiga SA, Flynn M, Lloyd AR, Weiser JN, Stubbs KA, Boraston AB, and King SJ. (2014). Unravelling the multiple functions of the architecturally intricate Streptococcus pneumoniae β-galactosidase, BgaA. PLoS Pathog. 2014;10(9):e1004364. DOI:10.1371/journal.ppat.1004364 | PubMed ID:25210925 [Singh2014]
  2. Boraston AB, Bolam DN, Gilbert HJ, and Davies GJ. (2004). Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 2004;382(Pt 3):769-81. DOI:10.1042/BJ20040892 | PubMed ID:15214846 [Boraston2004]
  3. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 | PubMed ID:18838391 [Cantarel209]

All Medline abstracts: PubMed