2JCD

Structure of the N-oxygenase AurF from Streptomyces thioluteus

2JCD の概要

• エントリーDOI: 10.2210/pdb2jcd/pdb
• 分子名称: N-OXIDASE, MANGANESE (II) ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: oxidation of p-benzoic acid, oxidoreductase, n-oxygenase, di-manganese mono-oxygenase
• 由来する生物種: STREPTOMYCES THIOLUTEUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78845.10

構造登録者

Zocher, G.E.,Winkler, R.,Hertweck, C.,Schulz, G.E. (登録日: 2006-12-21, 公開日: 2007-09-11, 最終更新日: 2024-05-08)

主引用文献

Zocher, G.E.,Winkler, R.,Hertweck, C.,Schulz, G.E.
Structure and Action of the N-Oxygenase Aurf from Streptomyces Thioluteus.
J.Mol.Biol., 373:65-, 2007

PubMed Abstract: Nitro groups are found in a number of bioactive compounds. Most of them arise by a stepwise mono-oxygenation of amino groups. One of the involved enzymes is AurF participating in the biosynthesis of aureothin. Its structure was established at 2.1 A resolution showing a homodimer with a binuclear manganese cluster. The enzyme preparation, which yielded the analyzed crystals, showed activity using in vitro and in vivo assays. Chain fold and cluster are homologous with ribonucleotide reductase subunit R2 and related enzymes. The two manganese ions and an iron content of about 15% were established by anomalous X-ray diffraction. A comparison of the cluster with more common di-iron clusters suggested an additional histidine in the coordination sphere to cause the preference for manganese over iron. There is no oxo-bridge. The substrate p-amino-benzoate was modeled into the active center. The model is supported by mutant activity measurements. It shows the geometry of the reaction and explains the established substrate spectrum.

PubMed: 17765264
DOI: 10.1016/J.JMB.2007.06.014

実験手法

X-RAY DIFFRACTION (2.11 Å)