6B6W

Crystal structure of Desulfovibrio vulgaris carbon monoxide dehydrogenase, as-isolated (protein batch 2), oxidized C-cluster

6B6W の概要

• エントリーDOI: 10.2210/pdb6b6w/pdb
• 分子名称: Carbon monoxide dehydrogenase, IRON/SULFUR CLUSTER, MAGNESIUM ION, ... (9 entities in total)
• 機能のキーワード: nickel-iron-sulfur (ni-fe-s) cluster, iron-sulfur (fe-s) cluster, metalloenzyme, oxidoreductase
• 由来する生物種: Desulfovibrio vulgaris
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 138488.73

構造登録者

Wittenborn, E.C.,Drennan, C.L. (登録日: 2017-10-03, 公開日: 2018-10-03, 最終更新日: 2023-10-04)

主引用文献

Wittenborn, E.C.,Merrouch, M.,Ueda, C.,Fradale, L.,Leger, C.,Fourmond, V.,Pandelia, M.E.,Dementin, S.,Drennan, C.L.
Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase.
Elife, 7:-, 2018

PubMed Abstract: The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have observed unprecedented conformational dynamics in the C-cluster of the CODH from , providing the first view of an oxidized state of the cluster. Combined with supporting spectroscopic data, our structures reveal that this novel, oxidized cluster arrangement plays a role in avoiding irreversible oxidative degradation at the C-cluster. Furthermore, mutagenesis of a conserved cysteine residue that binds the C-cluster in the oxidized state but not in the reduced state suggests that the oxidized conformation could be important for proper cluster assembly, in particular Ni incorporation. Together, these results lay a foundation for future investigations of C-cluster activation and assembly, and contribute to an emerging paradigm of metallocluster plasticity.

PubMed: 30277213
DOI: 10.7554/eLife.39451

実験手法

X-RAY DIFFRACTION (1.72 Å)