Eduardo Moreno Prieto: Structure comparison of families GH57 and GH119. (a) Superimposed Thermococcus litoralis GH57 4-a-glucanotransferase catalytic (b/a)7-barrel with succeeding ahelical segments (red; real structure; PDB code: 1K1Y [18]; residues M1-Q381) with Bacillus circulans GH119 a-amylase substantial part of the (b/a)7-barrel domain (blue; modelled structure; residues T121-D429). The superimposed part covers 228 Ca-atoms with a 0.66 Å root-mean square deviation. The rectangle indicates a detailed view on t...

2024-02-09T03:10:01Z

Structure comparison of families GH57 and GH119. (a) Superimposed Thermococcus litoralis GH57 4-a-glucanotransferase catalytic (b/a)7-barrel with succeeding ahelical segments (red; real structure; PDB code: 1K1Y [18]; residues M1-Q381) with Bacillus circulans GH119 a-amylase substantial part of the (b/a)7-barrel domain (blue; modelled structure; residues T121-D429). The superimposed part covers 228 Ca-atoms with a 0.66 Å root-mean square deviation. The rectangle indicates a detailed view on t...

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== Summary ==
Structure comparison of families GH57 and GH119. (a) Superimposed Thermococcus litoralis GH57 4-a-glucanotransferase catalytic (b/a)7-barrel with succeeding ahelical segments (red; real structure; PDB code: 1K1Y [18]; residues M1-Q381) with Bacillus circulans GH119 a-amylase substantial part of the (b/a)7-barrel domain (blue; modelled structure; residues T121-D429). The superimposed part covers 228 Ca-atoms with a 0.66 Å root-mean square deviation. The rectangle indicates a detailed view on the right. (b) A close-up focused on the catalytic residues in the structure of GH57 4-a-glucanotransferase (Glu123 and Asp214) and the proposed equivalent residues in the GH119 a-amylase (Glu231 and Asp373). Acarbose occupying subsites 1 through + 3 [40] in complex with GH57 4-a-glucanotransferase is shown. Source: Janeček et al. 2012, PubMed ID:22819817.

File:GH57 GH119 structure comparison.jpg - Revision history