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4YU5

Crystal structure of selenomethionine variant of Bacillus anthracis immune inhibitor A2 peptidase zymogen

4YU5 の概要
エントリーDOI10.2210/pdb4yu5/pdb
関連するPDBエントリー4YU6
分子名称Immune inhibitor A, metalloprotease, ZINC ION, CALCIUM ION, ... (7 entities in total)
機能のキーワードhydrolase, metallopeptidase, metzincin
由来する生物種Bacillus cereus var. anthracis (strain CI)
タンパク質・核酸の鎖数2
化学式量合計169734.74
構造登録者
Arolas, J.L.,Goulas, T.,Gomis-Ruth, F.X. (登録日: 2015-03-18, 公開日: 2015-10-28, 最終更新日: 2024-11-06)
主引用文献Arolas, J.L.,Goulas, T.,Pomerantsev, A.P.,Leppla, S.H.,Gomis-Ruth, F.X.
Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome.
Structure, 24:25-36, 2016
Cited by
PubMed Abstract: Immune inhibitor A(InhA)-type metallopeptidases are potential virulence factors secreted by members of the Bacillus cereus group. Two paralogs from anthrax-causing Bacillus anthracis (BaInhA1 and BaInhA2) were shown to degrade host tissue proteins with broad substrate specificity. Analysis of their activation mechanism and the crystal structure of a zymogenic BaInhA2 variant revealed a ∼750-residue four-domain structure featuring a pro-peptide, a catalytic domain, a domain reminiscent of viral envelope glycoproteins, and a MAM domain grafted into the latter. This domain, previously found only in eukaryotes, is required for proper protein expression in B. anthracis and evinces certain flexibility. Latency is uniquely modulated by the N-terminal segment of the pro-peptide, which binds the catalytic zinc through its α-amino group and occupies the primed side of the active-site cleft. The present results further our understanding of the modus operandi of an anthrax secretome regulator.
PubMed: 26745529
DOI: 10.1016/j.str.2015.10.015
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 4yu5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-09に公開中

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