4gf3

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gf3 OCA], [https://pdbe.org/4gf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gf3 RCSB], [https://www.ebi.ac.uk/pdbsum/4gf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gf3 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Yersinia pestis injects numerous bacterial proteins into host cells through an organic nanomachine called the type 3 secretion system. One such substrate is the tyrosine phosphatase YopH, which requires an interaction with a cognate chaperone in order to be effectively injected. Here, the first crystal structure of a SycH-YopH complex is reported, determined to 1.9 A resolution. The structure reveals the presence of (i) a nonglobular polypeptide in YopH, (ii) a so-called beta-motif in YopH and (iii) a conserved hydrophobic patch in SycH that recognizes the beta-motif. Biochemical studies establish that the beta-motif is critical to the stability of this complex. Finally, since previous work has shown that the N-terminal portion of YopH adopts a globular fold that is functional in the host cell, aspects of how this polypeptide adopts radically different folds in the host and in the bacterial environments are analysed.

Context-dependent protein folding of a virulence peptide in the bacterial and host environments: structure of an SycH-YopH chaperone-effector complex.,Vujanac M, Stebbins CE Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):546-54. doi:, 10.1107/S0907444912051086. Epub 2013 Mar 9. PMID:23519663<ref>PMID:23519663</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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