3NNF

Halogenase domain from CurA module with Fe, chloride, and alpha-ketoglutarate

3NNF の概要

• エントリーDOI: 10.2210/pdb3nnf/pdb
• 関連するPDBエントリー: 3NNJ 3NNL 3NNM
• 分子名称: CurA, FE (III) ION, FORMIC ACID, ... (6 entities in total)
• 機能のキーワード: non-haem fe(ii)/alpha-ketoglutarate-dependent enzymes, catalyzes a cryptic chlorination, biosynthetic protein
• 由来する生物種: Lyngbya majuscula
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40424.66

構造登録者

Khare, D.,Smith, J.L. (登録日: 2010-06-23, 公開日: 2010-07-28, 最終更新日: 2024-04-03)

主引用文献

Khare, D.,Wang, B.,Gu, L.,Razelun, J.,Sherman, D.H.,Gerwick, W.H.,Hakansson, K.,Smith, J.L.
Conformational switch triggered by alpha-ketoglutarate in a halogenase of curacin A biosynthesis
Proc.Natl.Acad.Sci.USA, 107:14099-14104, 2010

PubMed Abstract: The CurA halogenase (Hal) catalyzes a cryptic chlorination leading to cyclopropane ring formation in the synthesis of the natural product curacin A. Hal belongs to a family of enzymes that use Fe(2+), O(2) and alpha-ketoglutarate (alphaKG) to perform a variety of halogenation reactions in natural product biosynthesis. Crystal structures of the enzyme in five ligand states reveal strikingly different open and closed conformations dependent on alphaKG binding. The open form represents ligand-free enzyme, preventing substrate from entering the active site until both alphaKG and chloride are bound, while the closed form represents the holoenzyme with alphaKG and chloride coordinated to iron. Candidate amino acid residues involved in substrate recognition were identified by site-directed mutagenesis. These new structures provide direct evidence of a conformational switch driven by alphaKG leading to chlorination of an early pathway intermediate.

PubMed: 20660778
DOI: 10.1073/pnas.1006738107

実験手法

X-RAY DIFFRACTION (2.201 Å)