3KJE

Empty state of CooC1

3KJE の概要

• エントリーDOI: 10.2210/pdb3kje/pdb
• 関連するPDBエントリー: 3KJE 3KJH 3KJI
• 分子名称: CO dehydrogenase/acetyl-CoA synthase complex, accessory protein CooC (2 entities in total)
• 機能のキーワード: nickel binding protein, atpase, hydrolase, metal binding protein
• 由来する生物種: Carboxydothermus hydrogenoformans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27996.70

構造登録者

Jeoung, J.-H.,Dobbek, H. (登録日: 2009-11-03, 公開日: 2010-01-19, 最終更新日: 2024-02-21)

主引用文献

Jeoung, J.H.,Giese, T.,Grunwald, M.,Dobbek, H.
Crystal Structure of the ATP-Dependent Maturation Factor of Ni,Fe-Containing Carbon Monoxide Dehydrogenases
J.Mol.Biol., 396:1165-1179, 2010

PubMed Abstract: CooC proteins are ATPases involved in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenases. The genome of the carboxydotrophic bacterium Carboxydothermus hydrogenoformans encodes five carbon monoxide dehydrogenases and three CooC-type proteins, of which CooC1 was shown to be a nickel-binding ATPase. We determined the crystal structure of CooC1 in four different states: empty, ADP-bound, Zn(2+)/ADP-bound, and Zn(2+)-bound. The structure of CooC1 consists of two spatially separated functional modules: an ATPase module containing the deviant Walker A motif and a metal-binding module that confers the specific function of CooC1. The ATPase module is homologous to other members of the MinD family and, in analogy to the dimeric structure of ATP-bound Soj, is likely responsible for the ATP-dependent dimerization of CooC1. Its core topology classifies CooC1 as a member of the MinD family of SIMIBI (signal recognition particle, MinD and BioD)-class NTPases. The crystal structure of Zn(2+)-bound CooC1 reveals a conserved C-X-C motif as the metal-binding site responsible for metal-induced dimerization. The competitive binding of Ni(2+) and Zn(2+) to CooC1 in solution confirms that the conserved C-X-C motif is also responsible for the interaction with Ni(2+). A comparison of the different CooC1 structures determined suggests a mutual dependence of metal-binding site and nucleotide-binding site.

PubMed: 20064527
DOI: 10.1016/j.jmb.2009.12.062

実験手法

X-RAY DIFFRACTION (2.3 Å)