7WSX

Class III hybrid cluster protein (HCP) C67Y variant from Methanothermobacter marburgensis

7WSX の概要

• エントリーDOI: 10.2210/pdb7wsx/pdb
• 分子名称: Hydroxylamine reductase, FE-S-O HYBRID CLUSTER (3 entities in total)
• 機能のキーワード: hybrid cluster, iron-sulfur cluster, enzyme, reductase, metal binding protein, oxidoreductase
• 由来する生物種: Methanothermobacter marburgensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 113729.90

構造登録者

Fujishiro, T. (登録日: 2022-02-02, 公開日: 2023-02-08, 最終更新日: 2024-11-20)

主引用文献

Fujishiro, T.,Takaoka, K.
Class III hybrid cluster protein homodimeric architecture shows evolutionary relationship with Ni, Fe-carbon monoxide dehydrogenases.
Nat Commun, 14:5609-5609, 2023

PubMed Abstract: Hybrid cluster proteins (HCPs) are Fe-S-O cluster-containing metalloenzymes in three distinct classes (class I and II: monomer, III: homodimer), all of which structurally related to homodimeric Ni, Fe-carbon monoxide dehydrogenases (CODHs). Here we show X-ray crystal structure of class III HCP from Methanothermobacter marburgensis (Mm HCP), demonstrating its homodimeric architecture structurally resembles those of CODHs. Also, despite the different architectures of class III and I/II HCPs, [4Fe-4S] and hybrid clusters are found in equivalent positions in all HCPs. Structural comparison of Mm HCP and CODHs unveils some distinct features such as the environments of their homodimeric interfaces and the active site metalloclusters. Furthermore, structural analysis of Mm HCP C67Y and characterization of several Mm HCP variants with a Cys67 mutation reveal the significance of Cys67 in protein structure, metallocluster binding and hydroxylamine reductase activity. Structure-based bioinformatics analysis of HCPs and CODHs provides insights into the structural evolution of the HCP/CODH superfamily.

PubMed: 37709776
DOI: 10.1038/s41467-023-41289-4

実験手法

X-RAY DIFFRACTION (3 Å)