Biophysical and structural characterization of the putative nickel chaperone CooT from Carboxydothermus hydrogenoformans.
M AlfanoJ PérardR MirasP CattyChristine CavazzaPublished in: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry (2018)
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 [NiFe3S4] 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.
Keyphrases
- metal organic framework
- reduced graphene oxide
- oxide nanoparticles
- amino acid
- carbon nanotubes
- heat shock protein
- microbial community
- high resolution
- transcription factor
- wastewater treatment
- binding protein
- peripheral blood
- heat shock
- endoplasmic reticulum
- gold nanoparticles
- magnetic resonance
- ionic liquid
- computed tomography
- risk assessment
- climate change
- fluorescent probe