5n76 | pdb_00005n76

Crystal structure of the apo-form of the CO dehydrogenase accessory protein CooT from Rhodospirillum rubrum

spinqualitylabelsall models 5n76, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n76 is a 6 chain structure with sequence from "dicrospirillum_rubrum"_enderlein_1925 "dicrospirillum rubrum" enderlein 1925. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: cooT ("Dicrospirillum rubrum" Enderlein 1925) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed In Rhodospirillum rubrum, maturation of Carbon Monoxide Dehydrogenase (CODH) requires three accessory proteins, CooC, CooT and CooJ, dedicated to nickel insertion into the active site, which is constituted by a distorted [NiFe3S4] cubane coordinated with a mononuclear Fe site. CooC is an ATPase proposed to provide the energy required for the maturation process, while CooJ is described as a metallochaperone with 16 histidines and 2 cysteines at the C-terminus, likely involved in metal binding and/or storage. Prior to the present study, no information was available on CooT at the molecular level. Here, the X-ray structure of RrCooT was obtained, which revealed that this protein is a homodimer featuring a fold that resembles an Sm-like domain, suggesting a role in RNA metabolism that was however not supported by experimental observations. Biochemical and biophysical evidence based on circular dichroism spectroscopy, light scattering, isothermal titration calorimetry and site-directed mutagenesis showed that RrCooT specifically binds a single Ni(ii) per dimer, with a dissociation constant of 9 nM, through the pair of Cys2, highly conserved residues, located at the dimer interface. Despite its role in the activation of RrCODH in vivo, CooT was thought to be a unique protein, found only in R. rubrum, with an unclear function. In this study, we extended the biological impact of CooT, establishing that this protein is a member of a novel Ni(ii)-binding protein family with 111 homologues, linked to anaerobic metabolism in bacteria and archaea, and in most cases to the presence of CODH. The CO dehydrogenase accessory protein CooT is a novel nickel-binding protein.,Timm J, Brochier-Armanet C, Perard J, Zambelli B, Ollagnier-de-Choudens S, Ciurli S, Cavazza C Metallomics. 2017 Apr 27. doi: 10.1039/c7mt00063d. PMID:28447092 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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