1n5b | pdb_00001n5b

Crystal Structure Of The Yersinia enterocolitica Molecular Chaperone Syce

spinqualitylabelsall models 1n5b, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1n5b is a 4 chain structure with sequence from "bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939. This structure supersedes the now removed PDB entry 1md1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1jya, 1k6z, 1l2w, 1md1 Gene: YERA ("Bacterium enterocoliticum" Schleifstein and Coleman 1939) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [YERA_YERE8] Positive regulator of YopE. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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