1un1: Difference between revisions

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[[Category: xyloglucan]]
[[Category: xyloglucan]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:07:08 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:06:24 2007''

Revision as of 14:01, 30 October 2007

File:1un1.gif


1un1, resolution 2.10Å

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XYLOGLUCAN ENDOTRANSGLYCOSYLASE NATIVE STRUCTURE.

Overview

Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan, polymers in plant cell walls via a transglycosylation mechanism. Thus, XET, is a key enzyme in all plant processes that require cell wall remodeling., To provide a basis for detailed structure-function studies, the crystal, structure of Populus tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia pastoris, has been determined at 1.8-A, resolution. Even though the overall structure of PttXET16A is a curved, beta-sandwich similar to other enzymes in the glycoside hydrolase family, GH16, parts of its substrate binding cleft are more reminiscent of the, distantly related family GH7. In addition, XET has a C-terminal extension, that packs against the conserved core, providing an additional ... [(full description)]

About this Structure

1UN1 is a [Single protein] structure of sequence from [Populus tremula] with AU as [ligand]. Active as [Xyloglucan:xyloglucosyl transferase], with EC number [2.4.1.207]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding., Johansson P, Brumer H 3rd, Baumann MJ, Kallas AM, Henriksson H, Denman SE, Teeri TT, Jones TA, Plant Cell. 2004 Apr;16(4):874-86. Epub 2004 Mar 12. PMID:15020748

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