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2OLN

NikD, an unusual amino acid oxidase essential for nikkomycin biosynthesis: closed form at 1.15 A resolution

2OLN の概要
エントリーDOI10.2210/pdb2oln/pdb
関連するPDBエントリー2OLN 2OLO
分子名称nikD protein, SODIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
機能のキーワードflavoprotein, rossmann fold, oxidoreductase
由来する生物種Streptomyces tendae
タンパク質・核酸の鎖数1
化学式量合計45102.14
構造登録者
Carrell, C.J.,Bruckner, R.C.,Venci, D.,Zhao, G.,Jorns, M.S.,Mathews, F.S. (登録日: 2007-01-19, 公開日: 2007-07-31, 最終更新日: 2024-10-30)
主引用文献Carrell, C.J.,Bruckner, R.C.,Venci, D.,Zhao, G.,Jorns, M.S.,Mathews, F.S.
NikD, an unusual amino acid oxidase essential for nikkomycin biosynthesis: structures of closed and open forms at 1.15 and 1.90 A resolution
Structure, 15:928-941, 2007
Cited by
PubMed Abstract: NikD is an unusual amino-acid-oxidizing enzyme that contains covalently bound FAD, catalyzes a 4-electron oxidation of piperideine-2-carboxylic acid to picolinate, and plays a critical role in the biosynthesis of nikkomycin antibiotics. Crystal structures of closed and open forms of nikD, a two-domain enzyme, have been determined to resolutions of 1.15 and 1.9 A, respectively. The two forms differ by an 11 degrees rotation of the catalytic domain with respect to the FAD-binding domain. The active site is inaccessible to solvent in the closed form; an endogenous ligand, believed to be picolinate, is bound close to and parallel with the flavin ring, an orientation compatible with redox catalysis. The active site is solvent accessible in the open form, but the picolinate ligand is approximately perpendicular to the flavin ring and a tryptophan is stacked above the flavin ring. NikD also contains a mobile cation binding loop.
PubMed: 17697998
DOI: 10.1016/j.str.2007.06.010
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.15 Å)
構造検証レポート
Validation report summary of 2oln
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2025-03-05に公開中

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