Summary for 2JQA
| Entry DOI | 10.2210/pdb2jqa/pdb |
| Related | 1X9L |
| Descriptor | Hypothetical protein (1 entity in total) |
| Functional Keywords | copper binding protein, metal binding protein |
| Biological source | Deinococcus radiodurans |
| Total number of polymer chains | 1 |
| Total formula weight | 15492.15 |
| Authors | Banci, L.,Bertini, I.,Ciofi Baffoni, S.,Katsari, E.,Katsaros, N.,Kubicek, K. (deposition date: 2007-05-30, release date: 2007-06-12, Last modification date: 2023-12-20) |
| Primary citation | Banci, L.,Bertini, I.,Ciofi Baffoni, S.,Katsari, E.,Katsaros, N.,Kubicek, K.,Mangani, S. A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase Proc.Natl.Acad.Sci.USA, 102:3994-3999, 2005 Cited by PubMed Abstract: Sco1 and Cox17 are accessory proteins required for the correct assembly of eukaryotic cytochrome c oxidase. At variance with Sco1, Cox17 orthologs are found only in eukaryotes. We browsed bacterial genomes to search proteins functionally equivalent to Cox17, and we identified a class of proteins of unknown function displaying a conserved gene neighborhood to bacterial Sco1 genes, all sharing a potential metal binding motif H(M)X10MX21HXM. Two members of this group, DR1885 from Deinococcus radiodurans and CC3502 from Caulobacter crescentus, were expressed, and their interaction with copper was investigated. The solution structure and extended x-ray absorption fine structure data on the former protein reveal that the protein binds copper(I) through a histidine and three Mets in a cupredoxin-like fold. The surface location of the copper-binding site as well as the type of coordination are well poised for metal transfer chemistry, suggesting that DR1885 might transfer copper, taking the role of Cox17 in bacteria. On the basis of our results, a possible pathway for copper delivery to the Cu(A) center in bacteria is proposed. PubMed: 15753304DOI: 10.1073/pnas.0406150102 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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