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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 2
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pubmed:dateCreated |
2003-1-29
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0907-4449
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
389-92
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12554962-Amino Acid Sequence,
pubmed-meshheading:12554962-Bacterial Outer Membrane Proteins,
pubmed-meshheading:12554962-Bacterial Proteins,
pubmed-meshheading:12554962-Binding Sites,
pubmed-meshheading:12554962-Crystallography, X-Ray,
pubmed-meshheading:12554962-Dimerization,
pubmed-meshheading:12554962-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:12554962-Models, Molecular,
pubmed-meshheading:12554962-Trans-Activators,
pubmed-meshheading:12554962-Yersinia enterocolitica
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pubmed:year |
2003
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pubmed:articleTitle |
Structure of the Yersinia enterocolitica molecular-chaperone protein SycE.
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pubmed:affiliation |
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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