Context-dependent Protein Folding of a Virulence Peptide in the Bacterial and Host Environments: Structure of an SycH-YopH Chaperone-effector Complex

Overview

Journal Acta Crystallogr D Biol Crystallogr

Specialty Chemistry

Date 2013 Mar 23

PMID 23519663

Citations 8

Authors

Milos Vujanac

C Erec Stebbins

Affiliations

Soon will be listed here.

Abstract

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 Å resolution. The structure reveals the presence of (i) a nonglobular polypeptide in YopH, (ii) a so-called β-motif in YopH and (iii) a conserved hydrophobic patch in SycH that recognizes the β-motif. Biochemical studies establish that the β-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.

Citing Articles

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