2J74
Structure of Beta-1,4-Galactanase
Summary for 2J74
Entry DOI | 10.2210/pdb2j74/pdb |
Related | 1UR0 1UR4 2CCR |
Related PRD ID | PRD_900113 PRD_900114 |
Descriptor | YVFO, beta-D-galactopyranose-(1-4)-beta-D-galactopyranose-(1-4)-beta-D-galactopyranose, beta-D-galactopyranose-(1-4)-beta-D-galactopyranose, ... (5 entities in total) |
Functional Keywords | glycoside hydrolase family 53, hydrolase, gh-a, beta-1, galactan, 4-galactanase |
Biological source | BACILLUS LICHENIFORMIS |
Total number of polymer chains | 2 |
Total formula weight | 89330.49 |
Authors | Le Nours, J.,De Maria, L.,Welner, D.,Jorgensen, C.T.,Christensen, L.L.H.,Larsen, S.,Lo Leggio, L. (deposition date: 2006-10-06, release date: 2007-12-18, Last modification date: 2023-12-13) |
Primary citation | Le Nours, J.,De Maria, L.,Welner, D.,Jorgensen, C.T.,Christensen, L.L.H.,Borchert, T.V.,Larsen, S.,Lo Leggio, L. Investigating the Binding of Beta-1,4-Galactan to Bacillus Licheniformis Beta-1,4-Galactanase by Crystallography and Computational Modeling. Proteins, 75:977-, 2009 Cited by PubMed Abstract: Microbial beta-1,4-galactanases are glycoside hydrolases belonging to family 53, which degrade galactan and arabinogalactan side chains in the hairy regions of pectin, a major plant cell wall component. They belong to the larger clan GH-A of glycoside hydrolases, which cover many different poly- and oligosaccharidase specificities. Crystallographic complexes of Bacillus licheniformis beta-1,4-galactanase and its inactive nucleophile mutant have been obtained with methyl-beta(1-->4)-galactotetraoside, providing, for the first time, information on substrate binding to the aglycone side of the beta-1,4-galactanase substrate binding groove. Using the experimentally determined subsites as a starting point, a beta(1-->4)-galactononaose was built into the structure and subjected to molecular dynamics simulations giving further insight into the residues involved in the binding of the polysaccharide from subsite -4 to +5. In particular, this analysis newly identified a conserved beta-turn, which contributes to subsites -2 to +3. This beta-turn is unique to family 53 beta-1,4-galactanases among all clan GH-A families that have been structurally characterized and thus might be a structural signature for endo-beta-1,4-galactanase specificity. PubMed: 19089956DOI: 10.1002/PROT.22310 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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