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3BB7

Structure of Prevotella intermedia prointerpain A fragment 39-359 (mutant C154A)

3BB7 の概要
エントリーDOI10.2210/pdb3bb7/pdb
関連するPDBエントリー3BBA
分子名称interpain A (2 entities in total)
機能のキーワードcysteine protease, zymogen activation, bacterial odontopathogen, hydrolase
由来する生物種Prevotella intermedia
タンパク質・核酸の鎖数1
化学式量合計35062.93
構造登録者
主引用文献Mallorqui-Fernandez, N.,Manandhar, S.P.,Mallorqui-Fernandez, G.,Uson, I.,Wawrzonek, K.,Kantyka, T.,Sola, M.,Thogersen, I.B.,Enghild, J.J.,Potempa, J.,Gomis-Ruth, F.X.
A New Autocatalytic Activation Mechanism for Cysteine Proteases Revealed by Prevotella intermedia Interpain A
J.Biol.Chem., 283:2871-2882, 2008
Cited by
PubMed Abstract: Prevotella intermedia is a major periodontopathogen contributing to human gingivitis and periodontitis. Such pathogens release proteases as virulence factors that cause deterrence of host defenses and tissue destruction. A new cysteine protease from the cysteine-histidine-dyad class, interpain A, was studied in its zymogenic and self-processed mature forms. The latter consists of a bivalved moiety made up by two subdomains. In the structure of a catalytic cysteine-to-alanine zymogen variant, the right subdomain interacts with an unusual prodomain, thus contributing to latency. Unlike the catalytic cysteine residue, already in its competent conformation in the zymogen, the catalytic histidine is swung out from its active conformation and trapped in a cage shaped by a backing helix, a zymogenic hairpin, and a latency flap in the zymogen. Dramatic rearrangement of up to 20A of these elements triggered by a tryptophan switch occurs during activation and accounts for a new activation mechanism for proteolytic enzymes. These findings can be extrapolated to related potentially pathogenic cysteine proteases such as Streprococcus pyogenes SpeB and Porphyromonas gingivalis periodontain.
PubMed: 17993455
DOI: 10.1074/jbc.M708481200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 3bb7
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2024-10-30に公開中

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