1I78

CRYSTAL STRUCTURE OF OUTER MEMBRANE PROTEASE OMPT FROM ESCHERICHIA COLI

1I78 の概要

• エントリーDOI: 10.2210/pdb1i78/pdb
• 分子名称: PROTEASE VII, octyl beta-D-glucopyranoside, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: integral outer membrane protein, protease, beta barrel, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P09169
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68397.01

構造登録者

Vandeputte-Rutten, L.,Kramer, R.A.,Kroon, J.,Dekker, N.,Egmond, M.R.,Gros, P. (登録日: 2001-03-08, 公開日: 2001-10-03, 最終更新日: 2024-02-07)

主引用文献

Vandeputte-Rutten, L.,Kramer, R.A.,Kroon, J.,Dekker, N.,Egmond, M.R.,Gros, P.
Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.
EMBO J., 20:5033-5039, 2001

PubMed Abstract: OmpT from Escherichia coli belongs to a family of highly homologous outer membrane proteases, known as omptins, which are implicated in the virulence of several pathogenic Gram-negative bacteria. Here we present the crystal structure of OmpT, which shows a 10-stranded antiparallel beta-barrel that protrudes far from the lipid bilayer into the extracellular space. We identified a putative binding site for lipopolysaccharide, a molecule that is essential for OmpT activity. The proteolytic site is located in a groove at the extracellular top of the vase-shaped beta-barrel. Based on the constellation of active site residues, we propose a novel proteolytic mechanism, involving a His-Asp dyad and an Asp-Asp couple that activate a putative nucleophilic water molecule. The active site is fully conserved within the omptin family. Therefore, the structure described here provides a sound basis for the design of drugs against omptin-mediated bacterial pathogenesis. Coordinates are in the Protein Data Bank (accession No. 1I78)

PubMed: 11566868
DOI: 10.1093/emboj/20.18.5033

実験手法

X-RAY DIFFRACTION (2.6 Å)