6FAN

Crystal structure of putative CooT from Carboxydothermus hydrogenoformans

6FAN の概要

• エントリーDOI: 10.2210/pdb6fan/pdb
• 分子名称: CooT, (4S)-2-METHYL-2,4-PENTANEDIOL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: carbon monoxide dehydrogenase, nickel chaperone, maturation pathway, metal binding protein
• 由来する生物種: Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 44661.95

構造登録者

Cavazza, C.,Alfano, M. (登録日: 2017-12-15, 公開日: 2018-11-28, 最終更新日: 2024-05-08)

主引用文献

Alfano, M.,Perard, J.,Miras, R.,Catty, P.,Cavazza, C.
Biophysical and structural characterization of the putative nickel chaperone CooT from Carboxydothermus hydrogenoformans.
J.Biol.Inorg.Chem., 23:809-817, 2018

PubMed Abstract: Carboxydothermus hydrogenoformans is a model microorganism for the study of [NiFe]-CODH, a key enzyme of carbon cycle in anaerobic microorganisms. The enzyme possesses a unique active site (C-cluster), constituted of a distorted [NiFeS] cubane linked to a mononuclear Fe(II) center. Both the biogenesis of the C-cluster and the activation of CODH by nickel insertion remain unclear. Among the three accessory proteins thought to play a role in this latter step (CooC, CooJ, and CooT), CooT is identified as a nickel chaperone involved in CODH maturation in Rhodospirillum rubrum. Here, we structurally and biophysically characterized a putative CooT protein present in C. hydrogenoformans (pChCooT). Despite the low sequence homologies between CooT from R. rubrum (RrCooT) and pChCooT (19% sequence identity), the two proteins share several similarities, such as their overall structure and a solvent-exposed Ni(II)-binding site at the dimer interface. Moreover, the X-ray structure of pChCooT reveals the proximity between the histidine 55, a potential nickel-coordinating residue, and the cysteine 2, a highly conserved key residue in Ni(II)-binding.

PubMed: 29882029
DOI: 10.1007/s00775-018-1576-2

実験手法

X-RAY DIFFRACTION (2 Å)