4gf3

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.