2CCR

Structure of Beta-1,4-Galactanase

Summary for 2CCR

• Entry DOI: 10.2210/pdb2ccr/pdb
• Related: 1UR0 1UR4
• 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, ... (6 entities in total)
• Functional Keywords: beta-1, 4-galactanase, glycoside hydrolase family 53, gh-a, galactan, hydrolase
• Biological source: BACILLUS LICHENIFORMIS
• Total number of polymer chains: 2
• Total formula weight: 89630.84

Authors

Le Nours, J.,De Maria, L.,Welner, D.,Jorgensen, C.T.,Christensen, L.L.H.,Larsen, S.,Lo Leggio, L. (deposition date: 2006-01-18, release date: 2006-03-21, 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

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: 19089956
DOI: 10.1002/PROT.22310

Experimental method

X-RAY DIFFRACTION (2.3 Å)