Structure of the Yersinia enterocolitica molecular-chaperone protein SycE.
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.
Trame
Christine B
CB
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
McKay
David B
DB
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D019281:Dimerization; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D015534:Trans-Activators / Q000737:chemistry* / Q000378:metabolism; D015008:Yersinia enterocolitica / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; C081269:SycE protein, Yersinia; D015534:Trans-Activators; C063239:yopE protein, Yersinia