PDBsum entry: 2qom

Hydrolase

PDB id: 2qom

Contents

Protein chains

265 a.a. *

269 a.a. *

Waters ×6

* Residue conservation analysis

PDB id:

2qom

Name:

Hydrolase

Title:

The crystal structure of the e.Coli espp autotransporter bet

Structure:

Serine protease espp. Chain: a, b. Synonym: extracellular serine protease plasmid-encoded espp engineered: yes

Source:

Escherichia coli. Organism_taxid: 83334. Strain: o157:h7. Gene: espp. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.66Å R-factor: 0.260 R-free: 0.284

Authors:

T.J.Barnard,N.Dautin,P.Lukacik,H.D.Bernstein,S.K.Buchanan

Key ref:

T.J.Barnard et al. (2007). Autotransporter structure reveals intra-barrel cleavage followed by conformational changes. Nat Struct Mol Biol, 14, 1214-1220. PubMed id: 17994105 DOI: 10.1038/nsmb1322

Date:

20-Jul-07 Release date: 13-Nov-07

Protein chain

Q7BSW5  (ESPP_ECO57) -  Serine protease espP

Seq: 1300 a.a.

Struc: 265 a.a.

Protein chain

Q7BSW5  (ESPP_ECO57) -  Serine protease espP

Seq: 1300 a.a.

Struc: 269 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: outer membrane (1 term)

DOI no: 10.1038/nsmb1322

Nat Struct Mol Biol 14:1214-1220 (2007)

PubMed id: 17994105

Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.

T.J.Barnard, N.Dautin, P.Lukacik, H.D.Bernstein, S.K.Buchanan.

ABSTRACT

Autotransporters are virulence factors produced by Gram-negative bacteria. They consist of two domains, an N-terminal 'passenger' domain and a C-terminal beta-domain. beta-domains form beta-barrel structures in the outer membrane while passenger domains are translocated into the extracellular space. In some autotransporters, the two domains are separated by proteolytic cleavage. Using X-ray crystallography, we solved the 2.7-A structure of the post-cleavage state of the beta-domain of EspP, an autotransporter produced by Escherichia coli strain O157:H7. The structure consists of a 12-stranded beta-barrel with the passenger domain-beta-domain cleavage junction located inside the barrel pore, approximately midway between the extracellular and periplasmic surfaces of the outer membrane. The structure reveals an unprecedented intra-barrel cleavage mechanism and suggests that two conformational changes occur in the beta-domain after cleavage, one conferring increased stability on the beta-domain and another restricting access to the barrel pore.

Selected figure(s)

Figure 2.
Side chains of the residues forming the acidic cluster are shown as sticks. The -helix and linker loop are shown as an electrostatic surface (blue, positive; red, negative; white, neutral).

Figure 6.
(a) Two views of the electrostatic surface of the EspP barrel pore and luminal -helix with its linker loop (blue, positive; red, negative; white, neutral). The barrel pore is notably acidic. (b) Two views of the electrostatic surface of the NalP barrel pore and luminal -helix with its linker loop. Unlike the interior of the EspP -barrel, the interior of the NalP -barrel has an asymmetric charge distribution, basic toward the periplasm and acidic or neutral toward the extracellular surface.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2007, 14, 1214-1220) copyright 2007.

Figures were selected by an automated process.