1e5c

From Proteopedia

Revision as of 13:01, 30 October 2007

INTERNAL XYLAN BINDING DOMAIN FROM C. FIMI XYN10A, R262G MUTANT

Overview

The interactions of proteins with polysaccharides play a key role in the, microbial hydrolysis of cellulose and xylan, the most abundant organic, molecules in the biosphere, and are thus pivotal to the recycling of, photosynthetically fixed carbon. Enzymes that attack these recalcitrant, polymers have a modular structure comprising catalytic modules and, non-catalytic carbohydrate-binding modules (CBMs). The largest prokaryotic, CBM family, CBM2, contains members that bind cellulose (CBM2a) and xylan, (CBM2b), respectively. A possible explanation for the different ligand, specificity of CBM2b is that one of the surface tryptophans involved in, the protein-carbohydrate interaction is rotated by 90 degrees compared, with its position in CBM2a (thus matching the structure of the binding, ... [(full description)]

About this Structure

1E5C is a [Single protein] structure of sequence from [Cellulomonas fimi]. Active as [Endo-1,4-beta-xylanase], with EC number [3.2.1.8]. Structure known Active Site: XBD. Full crystallographic information is available from [OCA].

Reference

The structural basis for the ligand specificity of family 2 carbohydrate-binding modules., Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP, J Biol Chem. 2000 Dec 29;275(52):41137-42. PMID:10973978

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