6fan | pdb_00006fan

Crystal structure of putative CooT from Carboxydothermus hydrogenoformans

spinqualitylabelsall models 6fan, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fan is a 6 chain structure with sequence from Carboxydothermus hydrogenoformans Z-2901. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: GOL, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3AFN4_CARHZ Publication Abstract from PubMed 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. Biophysical and structural characterization of the putative nickel chaperone CooT from Carboxydothermus hydrogenoformans.,Alfano M, Perard J, Miras R, Catty P, Cavazza C J Biol Inorg Chem. 2018 Jun 7. pii: 10.1007/s00775-018-1576-2. doi:, 10.1007/s00775-018-1576-2. PMID:29882029 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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