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Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):389-92. Epub 2003 Jan 23.

Structure of the Yersinia enterocolitica molecular-chaperone protein SycE.

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  • 1Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.


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.

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