7TSJ

Xenon-bound structure of carbon monoxide dehydrogenase (CODH) from Desulfovibrio vulgaris

7TSJ の概要

• エントリーDOI: 10.2210/pdb7tsj/pdb
• 分子名称: Carbon monoxide dehydrogenase, IRON/SULFUR CLUSTER, FE2/S2 (INORGANIC) CLUSTER, ... (6 entities in total)
• 機能のキーワード: co-dehydrogenase, desulfovibrio vulgaris, xenon, oxidoreductase
• 由来する生物種: Desulfovibrio vulgaris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 70229.21

構造登録者

Biester, A.,Drennan, C.L. (登録日: 2022-01-31, 公開日: 2022-05-04, 最終更新日: 2023-10-18)

主引用文献

Biester, A.,Dementin, S.,Drennan, C.L.
Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase.
J.Inorg.Biochem., 230:111774-111774, 2022

PubMed Abstract: Carbon monoxide dehydrogenase (CODH) plays an important role in the processing of the one‑carbon gases carbon monoxide and carbon dioxide. In CODH enzymes, these gases are channeled to and from the Ni-Fe-S active sites using hydrophobic cavities. In this work, we investigate these gas channels in a monofunctional CODH from Desulfovibrio vulgaris, which is unusual among CODHs for its oxygen-tolerance. By pressurizing D. vulgaris CODH protein crystals with xenon and solving the structure to 2.10 Å resolution, we identify 12 xenon sites per CODH monomer, thereby elucidating hydrophobic gas channels. We find that D. vulgaris CODH has one gas channel that has not been experimentally validated previously in a CODH, and a second channel that is shared with Moorella thermoacetica carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS). This experimental visualization of D. vulgaris CODH gas channels lays groundwork for further exploration of factors contributing to oxygen-tolerance in this CODH, as well as study of channels in other CODHs. We dedicate this publication to the memory of Dick Holm, whose early studies of the Ni-Fe-S clusters of CODH inspired us all.

PubMed: 35278753
DOI: 10.1016/j.jinorgbio.2022.111774

実験手法

X-RAY DIFFRACTION (2.1 Å)