3NJH

D37A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis.

3NJH の概要

• エントリーDOI: 10.2210/pdb3njh/pdb
• 関連するPDBエントリー: 3N55 3NJF 3NJG 3NJI 3NJJ 3NJK 3NJL 3NJM 3NJN
• 分子名称: Peptidase, CALCIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: structural genomics, aspartic peptidase, autocatalysis, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase
• 由来する生物種: Shewanella oneidensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 55028.51

構造登録者

Osipiuk, J.,Mulligan, R.,Bargassa, M.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2010-06-17, 公開日: 2010-07-14, 最終更新日: 2023-09-06)

主引用文献

Osipiuk, J.,Mulligan, R.,Bargassa, M.,Hamilton, J.E.,Cunningham, M.A.,Joachimiak, A.
Characterization of member of DUF1888 protein family, self-cleaving and self-assembling endopeptidase.
J.Biol.Chem., 287:19452-19461, 2012

PubMed Abstract: The crystal structure of SO1698 protein from Shewanella oneidensis was determined by a SAD method and refined to 1.57 Å. The structure is a β sandwich that unexpectedly consists of two polypeptides; the N-terminal fragment includes residues 1-116, and the C-terminal one includes residues 117-125. Electron density also displayed the Lys-98 side chain covalently linked to Asp-116. The putative active site residues involved in self-cleavage were identified; point mutants were produced and characterized structurally and in a biochemical assay. Numerical simulations utilizing molecular dynamics and hybrid quantum/classical calculations suggest a mechanism involving activation of a water molecule coordinated by a catalytic aspartic acid.

PubMed: 22493430
DOI: 10.1074/jbc.M112.358069

実験手法

X-RAY DIFFRACTION (1.94 Å)