6J1I

Crystal structure of HypX from Aquifex aeolicus, A392F-I419F variant

6J1I の概要

• エントリーDOI: 10.2210/pdb6j1i/pdb
• 関連するPDBエントリー: 6J0P
• 分子名称: Hydrogenase regulation HoxX, COENZYME A, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: hydrogenase, maturation, carbon monoxide, biosynthetic protein
• 由来する生物種: Aquifex aeolicus VF5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68736.18

構造登録者

Muraki, N.,Aono, S. (登録日: 2018-12-28, 公開日: 2019-11-06, 最終更新日: 2023-11-22)

主引用文献

Muraki, N.,Ishii, K.,Uchiyama, S.,Itoh, S.G.,Okumura, H.,Aono, S.
Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.
Commun Biol, 2:385-385, 2019

PubMed Abstract: Several accessory proteins are required for the assembly of the metal centers in hydrogenases. In NiFe-hydrogenases, CO and CN are coordinated to the Fe in the NiFe dinuclear cluster of the active center. Though these diatomic ligands are biosynthesized enzymatically, detail mechanisms of their biosynthesis remain unclear. Here, we report the structural characterization of HypX responsible for CO biosynthesis to assemble the active site of NiFe hydrogenase. CoA is constitutionally bound in HypX. Structural characterization of HypX suggests that the formyl-group transfer will take place from N-formyl-THF to CoA to form formyl-CoA in the N-terminal domain of HypX, followed by decarbonylation of formyl-CoA to produce CO in the C-terminal domain though the direct experimental results are not available yet. The conformation of CoA accommodated in the continuous cavity connecting the N- and C-terminal domains will interconvert between the extended and the folded conformations for HypX catalysis.

PubMed: 31646188
DOI: 10.1038/s42003-019-0631-z

実験手法

X-RAY DIFFRACTION (2.29 Å)