1n5b
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(New page: 200px<br /><applet load="1n5b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n5b, resolution 2.00Å" /> '''Crystal Structure Of...)
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Revision as of 19:51, 20 November 2007
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Crystal Structure Of The Yersinia enterocolitica Molecular Chaperone Syce
Overview
The crystal structure of the Yersinia enterocolitica molecular-chaperone, protein SycE, which specifically binds the YopE protein, has been solved, to 2.0 A resolution by molecular replacement. The crystal contains two, SycE dimers per asymmetric unit; a novel feature of this crystal, when, compared with closely related SycE structures, is a well ordered, carboxy-terminal peptide in one protomer of each dimer. The peptide binds, a hydrophobic patch of a neighboring molecule in a manner similar to that, seen in a SycE-YopE chaperone-target complex, suggestive of low-affinity, 'self-binding' through which the carboxy-terminal peptide might suppress, counterproductive interactions with non-target proteins in vivo.
About this Structure
1N5B is a Single protein structure of sequence from Yersinia enterocolitica. This structure superseeds the now removed PDB entry 1MD1. Full crystallographic information is available from OCA.
Reference
Structure of the Yersinia enterocolitica molecular-chaperone protein SycE., Trame CB, McKay DB, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):389-92. Epub 2003, Jan 23. PMID:12554962
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