3N55

SO1698 protein, an aspartic peptidase from Shewanella oneidensis.

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3N55 の概要

• エントリーDOI: 10.2210/pdb3n55/pdb
• 分子名称: Peptidase, BETA-MERCAPTOETHANOL, ACETATE ION, ... (6 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; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14040.93

構造登録者

Osipiuk, J.,Mulligan, R.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2010-05-24, 公開日: 2010-06-02, 最終更新日: 2025-03-26)

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 (1.57 Å)