2QOM

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

2QOM の概要

• エントリーDOI: 10.2210/pdb2qom/pdb
• 分子名称: Serine protease espP (2 entities in total)
• 機能のキーワード: outer membrane protein, beta-barrel, beta-domain, autotransporter, hydrolase, protease, secreted, serine protease, transmembrane, virulence, zymogen
• 由来する生物種: Escherichia coli
• 細胞内の位置: Serine protease EspP: Periplasm . Secreted autotransporter protein EspP: Secreted. Autotransporter protein EspP translocator: Cell outer membrane ; Multi-pass membrane protein : Q7BSW5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62673.10

構造登録者

Barnard, T.J.,Dautin, N.,Lukacik, P.,Bernstein, H.D.,Buchanan, S.K. (登録日: 2007-07-20, 公開日: 2007-11-13, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.66 Å)