2QOM

The crystal structure of the E.coli EspP autotransporter Beta-domain.

Summary for 2QOM

• Entry DOI: 10.2210/pdb2qom/pdb
• Descriptor: Serine protease espP (2 entities in total)
• Functional Keywords: outer membrane protein, beta-barrel, beta-domain, autotransporter, hydrolase, protease, secreted, serine protease, transmembrane, virulence, zymogen
• Biological source: Escherichia coli
• Cellular location: Serine protease EspP: Periplasm . Secreted autotransporter protein EspP: Secreted. Autotransporter protein EspP translocator: Cell outer membrane ; Multi-pass membrane protein : Q7BSW5
• Total number of polymer chains: 2
• Total formula weight: 62673.10

Authors

Barnard, T.J.,Dautin, N.,Lukacik, P.,Bernstein, H.D.,Buchanan, S.K. (deposition date: 2007-07-20, release date: 2007-11-13, Last modification date: 2024-04-03)

Primary citation

Barnard, T.J.,Dautin, N.,Lukacik, P.,Bernstein, H.D.,Buchanan, S.K.
Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.
Nat.Struct.Mol.Biol., 14:1214-1220, 2007

PubMed 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.

PubMed: 17994105
DOI: 10.1038/nsmb1322

Experimental method

X-RAY DIFFRACTION (2.66 Å)