2k6y
Solution structures of apo form PCuA (cis conformation of the peptide bond involving the nitrogen of P14)Solution structures of apo form PCuA (cis conformation of the peptide bond involving the nitrogen of P14)
Structural highlights
FunctionEvolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCopper is essential for proper functioning of cytochrome c oxidases, and therefore for cellular respiration in eukaryotes and many bacteria. Here we show that a new periplasmic protein (PCu(A)C) selectively inserts Cu(I) ions into subunit II of Thermus thermophilus ba(3) oxidase to generate a native Cu(A) site. The purported metallochaperone Sco1 is unable to deliver copper ions; instead, it works as a thiol-disulfide reductase to maintain the correct oxidation state of the Cu(A) cysteine ligands. Mechanism of Cu(A) assembly.,Abriata LA, Banci L, Bertini I, Ciofi-Baffoni S, Gkazonis P, Spyroulias GA, Vila AJ, Wang S Nat Chem Biol. 2008 Oct;4(10):599-601. Epub 2008 Aug 31. PMID:18758441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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