PDBsum entry 2xcc

Protein binding

PDB id: 2xcc

Contents

Protein chains

133 a.a. *

Waters ×28

* Residue conservation analysis

PDB id:

2xcc

Name:

Protein binding

Title:

Crystal structure of pcrh from pseudomonas aeruginosa

Structure:

Regulatory protein pcrh. Chain: a, b. Fragment: residues 21-160. Synonym: pcrh. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.13Å R-factor: 0.262 R-free: 0.296

Authors:

V.Job,P.-J.Mattei,D.Lemaire,I.Attree,A.Dessen

Key ref:

V.Job et al. (2010). Structural basis of chaperone recognition of type III secretion system minor translocator proteins. J Biol Chem, 285, 23224-23232. PubMed id: 20385547

Date:

22-Apr-10 Release date: 05-May-10

Protein chains

Q9I325  (Q9I325_PSEAE) -  Regulatory protein PcrH from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 167 a.a.

Struc: 133 a.a.

J Biol Chem 285:23224-23232 (2010)

PubMed id: 20385547

Structural basis of chaperone recognition of type III secretion system minor translocator proteins.

V.Job, P.J.Matteï, D.Lemaire, I.Attree, A.Dessen.

ABSTRACT

The type III secretion system (T3SS) is a complex nanomachine employed by many Gram-negative pathogens, including the nosocomial agent Pseudomonas aeruginosa, to inject toxins directly into the cytoplasm of eukaryotic cells. A key component of all T3SS is the translocon, a proteinaceous channel that is inserted into the target membrane, which allows passage of toxins into target cells. In most bacterial species, two distinct membrane proteins (the translocators) are involved in translocon formation; whilst in the bacterial cytoplasm, however, they remain associated to a common chaperone. To date, the strategy employed by a single chaperone to recognize two distinct translocators is unknown. Here, we report the crystal structure of a complex between the Pseudomonas translocator chaperone PcrH and a short region from the minor translocator PopD. PcrH displays a 7-helical tetratricopeptide repeat (TPR) fold that harbors the PopD peptide within its concave region, originally believed to be involved in recognition of the major translocator, PopB. Point mutations introduced into the PcrH-interacting region of PopD impede translocator-chaperone recognition in vitro and lead to impairment of bacterial cytotoxicity towards macrophages in vivo. These results indicate that T3SS translocator chaperones form binary complexes with their partner molecules, and the stability of their interaction regions must be strictly maintained in order to guarantee bacterial infectivity. The PcrH-PopD complex displays homologs amongst a number of pathogenic strains, and could represent a novel, potential target for antibiotic development.