PDBsum entry 2os7

Chaperone

PDB id: 2os7

Contents

Protein chains

206 a.a. *

196 a.a. *

* Residue conservation analysis

PDB id:

2os7

Name:

Chaperone

Title:

Caf1m periplasmic chaperone tetramer

Structure:

Chaperone protein caf1m. Chain: a, b, c, d, e, f. Synonym: capsule protein fraction 1. Engineered: yes

Source:

Yersinia pestis. Organism_taxid: 632. Gene: caf1m. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.90Å R-factor: 0.252 R-free: 0.298

Authors:

S.D.Knight,A.Z.Zavialov

Key ref:

A.V.Zavialov and S.D.Knight (2007). A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M. Mol Microbiol, 64, 153-164. PubMed id: 17376079

Date:

05-Feb-07 Release date: 17-Apr-07

Protein chains

P26926  (CAF1M_YERPE) -  Chaperone protein caf1M from Yersinia pestis

Seq: 258 a.a.

Struc: 206 a.a.

Protein chains

P26926  (CAF1M_YERPE) -  Chaperone protein caf1M from Yersinia pestis

Seq: 258 a.a.

Struc: 196 a.a.

Mol Microbiol 64:153-164 (2007)

PubMed id: 17376079

A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M.

A.V.Zavialov, S.D.Knight.

ABSTRACT

The chaperone Caf1M belongs to a family of ATP-independent periplasmic chaperones that together with outer membrane ushers assemble and secrete filamentous adhesion organelles in Gram-negative pathogens. It assists in folding and transport of Caf1 subunits of the F1 capsular antigen of Yersinia pestis, the microbe causing bubonic plague. In the periplasm, Caf1M prevents subunit aggregation by capping the extensive hydrophobic surface of activated Caf1. We found that subunit-free Caf1M exists predominantly as a tetramer [K(d) = (2-30) x 10(-14) M(3) in the 12-37 degrees C interval]. A 2.9 A resolution crystal structure of the Caf1M tetramer reveals that each of the four molecules contribute its subunit binding sequences (the A(1) and G(1) strands) to form an eight-stranded hetero-sandwich with a well-packed phenylalanine-rich hydrophobic core. Tetramerization protects chaperone molecules against enzymatic proteolysis. Deletions in the subunit binding motifs completely abolish tetramer assembly, suggesting that the hetero-sandwich is the main structural feature holding the tetramer together. Arresting tetramer assembly by a deletion of the N-terminal binding motif, while leaving the major subunit binding motif VGVFVQFAI (G(1) strand) intact, results in accumulation of unspecific aggregates. Deletions in the VGVFVQFAI motif abolish both tetramer assembly and aggregation, consistent with the predicted high beta-aggregation propensity for this motif. These results suggest that the packing of the aggregation-prone subunit binding sequences into the hetero-domain is a novel molecular mechanism preventing unspecific aggregation of the free chaperone.