4GF3

Structure of a SycH-YopH Chaperone-Effector Complex

Summary for 4GF3

• Entry DOI: 10.2210/pdb4gf3/pdb
• Descriptor: Putative yopH targeting protein, Tyrosine-protein phosphatase yopH (3 entities in total)
• Functional Keywords: t3ss chaperone, chaperone-chaperone effector complex, chaperone/chaperone effector
• Biological source: Yersinia pestis; More
• Cellular location: Secreted: P15273
• Total number of polymer chains: 2
• Total formula weight: 20278.96

Authors

Stebbins, C.E.,Vujanac, M. (deposition date: 2012-08-02, release date: 2013-03-27, Last modification date: 2024-02-28)

Primary citation

Vujanac, M.,Stebbins, C.E.
Context-dependent protein folding of a virulence peptide in the bacterial and host environments: structure of an SycH-YopH chaperone-effector complex.
Acta Crystallogr.,Sect.D, 69:546-554, 2013

PubMed 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.

PubMed: 23519663
DOI: 10.1107/S0907444912051086

Experimental method

X-RAY DIFFRACTION (1.9 Å)