Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2UXY

Aliphatic amidase

2UXY の概要
エントリーDOI10.2210/pdb2uxy/pdb
関連するPDBエントリー1K17
分子名称ALIPHATIC AMIDASE, SULFATE ION (3 entities in total)
機能のキーワードnitrilase superfamily, pseudomonas aeruginosa, hydrolase, acyl transfer, thiol enzymes, hydroxamic acid, aliphatic amidase
由来する生物種PSEUDOMONAS AERUGINOSA
タンパク質・核酸の鎖数1
化学式量合計38136.18
構造登録者
Andrade, J.,KArmali, A.,Carrondo, M.A.,Frazao, C. (登録日: 2007-04-02, 公開日: 2007-04-17, 最終更新日: 2025-04-09)
主引用文献Andrade, J.,Karmali, A.,Carrondo, M.A.,Frazao, C.
Structure of Amidase from Pseudomonas Aeruginosa Showing a Trapped Acyl Transfer Reaction Intermediate State.
J.Biol.Chem., 282:19598-, 2007
Cited by
PubMed Abstract: Microbial amidases belong to the thiol nitrilases family and have potential biotechnological applications in chemical and pharmaceutical industries as well as in bioremediation. The amidase from Pseudomonas aeruginosa isa6 x 38-kDa enzyme that catalyzes the hydrolysis of a small range of short aliphatic amides. The hereby reported high resolution crystallographic structure shows that each amidase monomer is formed by a globular four-layer alphabetabetaalpha sandwich domain with an additional 81-residue long C-terminal segment. This wraps arm-in-arm with a homologous C-terminal chain of another monomer, producing a strongly packed dimer. In the crystal, the biological active homo-hexameric amidase is built grouping three such dimers around a crystallographic 3-fold axis. The structure also elucidates the structural basis for the enzyme activity, with the nitrilases catalytic triad at the bottom of a 13-A deep, funnel-shaped pocket, accessible from the solvent through a narrow neck with 3-A diameter. An acyl transfer intermediate, resulting from the purification protocol, was found bound to the amidase nucleophilic agent, Cys(166). These results suggest that some pocket defining residues should undergo conformational shifts to allow substrates and products to access and leave the catalytic pocket, for turnover to occur.
PubMed: 17442671
DOI: 10.1074/JBC.M701039200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.25 Å)
構造検証レポート
Validation report summary of 2uxy
検証レポート(詳細版)ダウンロードをダウンロード

252456

件を2026-04-22に公開中

PDB statisticsPDBj update infoContact PDBjnumon