2k6v

Solution structures of apo Sco1 protein from Thermus ThermophilusSolution structures of apo Sco1 protein from Thermus Thermophilus

Structural highlights 2k6v is a 1 chain structure with sequence from Thermus thermophilus HB8. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5SGY8_THET8 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Copper 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2k6v Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image