1un1

From Proteopedia

Revision as of 18:06, 29 October 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1un1, resolution 2.10Å

Drag the structure with the mouse to rotate

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 [[1]], with EC number [2.4.1.207]. 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

Page seeded by OCA on Mon Oct 29 20:11:20 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools