3C7F

Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from bacillus subtilis in complex with xylotriose.

Summary for 3C7F

• Entry DOI: 10.2210/pdb3c7f/pdb
• Related: 3C7E 3C7G 3C7H 3C7O
• Related PRD ID: PRD_900117
• Descriptor: Endo-1,4-beta-xylanase, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: 5-bladed beta-propeller fold, beta-sandwich, xylan degradation, hydrolase
• Biological source: Bacillus subtilis
• Cellular location: Secreted: Q45071
• Total number of polymer chains: 1
• Total formula weight: 52867.06

Authors

Vandermarliere, E.,Bourgois, T.M.,Winn, M.D.,Van Campenhout, S.,Volckaert, G.,Strelkov, S.V.,Delcour, J.A.,Rabijns, A.,Courtin, C.M. (deposition date: 2008-02-07, release date: 2008-11-18, Last modification date: 2023-08-30)

Primary citation

Vandermarliere, E.,Bourgois, T.M.,Winn, M.D.,van Campenhout, S.,Volckaert, G.,Delcour, J.A.,Strelkov, S.V.,Rabijns, A.,Courtin, C.M.
Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family.
Biochem.J., 418:39-47, 2009

PubMed Abstract: AXHs (arabinoxylan arabinofuranohydrolases) are alpha-L-arabinofuranosidases that specifically hydrolyse the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis was recently shown to produce an AXH that cleaves arabinose units from O-2- or O-3-mono-substituted xylose residues: BsAXH-m2,3 (B. subtilis AXH-m2,3). Crystallographic analysis reveals a two-domain structure for this enzyme: a catalytic domain displaying a five-bladed beta-propeller fold characteristic of GH (glycoside hydrolase) family 43 and a CBM (carbohydrate-binding module) with a beta-sandwich fold belonging to CBM family 6. Binding of substrate to BsAXH-m2,3 is largely based on hydrophobic stacking interactions, which probably allow the positional flexibility needed to hydrolyse both arabinose substituents at the O-2 or O-3 position of the xylose unit. Superposition of the BsAXH-m2,3 structure with known structures of the GH family 43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone.

PubMed: 18980579
DOI: 10.1042/BJ20081256

Experimental method

X-RAY DIFFRACTION (1.55 Å)