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3SZE

Crystal structure of the passenger domain of the E. coli autotransporter EspP

3SZE の概要
エントリーDOI10.2210/pdb3sze/pdb
分子名称Serine protease espP (2 entities in total)
機能のキーワードparallel beta-helix, serine protease, hydrolase
由来する生物種Escherichia coli O157:H7
細胞内の位置Serine protease espP: Periplasm (By similarity). Secreted autotransporter protein espP: Secreted. Autotransporter protein espP translocator: Cell outer membrane; Multi-pass membrane protein (By similarity): Q7BSW5
タンパク質・核酸の鎖数1
化学式量合計105535.26
構造登録者
Khan, S.,Mian, H.S.,Sandercock, L.E.,Battaile, K.P.,Lam, R.,Chirgadze, N.Y.,Pai, E.F. (登録日: 2011-07-18, 公開日: 2011-10-12, 最終更新日: 2024-02-28)
主引用文献Khan, S.,Mian, H.S.,Sandercock, L.E.,Chirgadze, N.Y.,Pai, E.F.
Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP.
J.Mol.Biol., 413:985-1000, 2011
Cited by
PubMed Abstract: Autotransporters represent a large superfamily of known and putative virulence factors produced by Gram-negative bacteria. They consist of an N-terminal "passenger domain" responsible for the specific effector functions of the molecule and a C-terminal "β-domain" responsible for translocation of the passenger across the bacterial outer membrane. Here, we present the 2.5-Å crystal structure of the passenger domain of the extracellular serine protease EspP, produced by the pathogen Escherichia coli O157:H7 and a member of the serine protease autotransporters of Enterobacteriaceae (SPATEs). Like the previously structurally characterized SPATE passenger domains, the EspP passenger domain contains an extended right-handed parallel β-helix preceded by an N-terminal globular domain housing the catalytic function of the protease. Of note, however, is the absence of a second globular domain protruding from this β-helix. We describe the structure of the EspP passenger domain in the context of previous results and provide an alternative hypothesis for the function of the β-helix within SPATEs.
PubMed: 21964244
DOI: 10.1016/j.jmb.2011.09.028
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 3sze
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件を2025-12-31に公開中

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