1heh

From Proteopedia

Revision as of 13:30, 30 October 2007

C-TERMINAL XYLAN BINDING DOMAIN FROM CELLULOMONAS FIMI XYLANASE 11A

Overview

Glycoside hydrolases often contain multiple copies of noncatalytic, carbohydrate binding modules (CBMs) from the same or different families., Currently, the functional importance of this complex molecular, architecture is unclear. To investigate the role of multiple CBMs in plant, cell wall hydrolases, we have determined the polysaccharide binding, properties of wild type and various derivatives of Cellulomonas fimi, xylanase 11A (Cf Xyn11A). This protein, which binds to both cellulose and, xylan, contains two family 2b CBMs that exhibit 70% sequence identity, one, internal (CBM2b-1), which has previously been shown to bind specifically, to xylan and the other at the C-terminus (CBM2b-2). Biochemical, characterization of CBM2b-2 showed that the module bound to insoluble and, soluble oat ... [(full description)]

About this Structure

1HEH 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

Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A., Bolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ, Biochemistry. 2001 Feb 27;40(8):2468-77. PMID:11327868

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