1W0N

Structure of uncomplexed Carbohydrate Binding Domain CBM36

Summary for 1W0N

• Entry DOI: 10.2210/pdb1w0n/pdb
• Related: 1UX7
• Descriptor: ENDO-1,4-BETA-XYLANASE D, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase, carbohydrate-binding module, carbohydrate binding, xylan, cbm36, xylanase
• Biological source: PAENIBACILLUS POLYMYXA
• Total number of polymer chains: 1
• Total formula weight: 14041.62

Authors

Jamal, S.,Boraston, A.B.,Davies, G.J. (deposition date: 2004-06-09, release date: 2004-10-27, Last modification date: 2024-05-08)

Primary citation

Jamal, S.,Boraston, A.B.,Turkenburg, J.P.,Tarbouriech, N.,Ducros, V.M.-A.,Davies, G.J.
Ab Initio Structure Determination and Functional Characterization of Cbm36: A New Family of Calcium-Dependent Carbohydrate Binding Modules
Structure, 12:1177-, 2004

PubMed Abstract: The enzymatic degradation of polysaccharides harnesses multimodular enzymes whose carbohydrate binding modules (CBM) target the catalytic domain onto the recalcitrant substrate. Here we report the ab initio structure determination and subsequent refinement, at 0.8 A resolution, of the CBM36 domain of the Paenibacillus polymyxa xylanase 43A. Affinity electrophoresis, isothermal titration calorimetry, and UV difference spectroscopy demonstrate that CBM36 is a novel Ca(2+)-dependent xylan binding domain. The 3D structure of CBM36 in complex with xylotriose and Ca(2+), at 1.5 A resolution, displays significant conformational changes compared to the native structure and reveals the molecular basis for its unique Ca(2+)-dependent binding of xylooligosaccharides through coordination of the O2 and O3 hydroxyls. CBM36 is one of an emerging spectrum of carbohydrate binding modules that increasingly find applications in industry and display great potential for mapping the "glyco-architecture" of plant cells.

PubMed: 15242594
DOI: 10.1016/J.STR.2004.04.022

Experimental method

X-RAY DIFFRACTION (0.8 Å)