2K6V

Solution structures of apo Sco1 protein from Thermus Thermophilus

Summary for 2K6V

• Entry DOI: 10.2210/pdb2k6v/pdb
• Related: 2K6W 2K6Y 2K6Z 2K70
• NMR Information: BMRB: 15893
• Descriptor: Putative cytochrome c oxidase assembly protein (1 entity in total)
• Functional Keywords: thioredoxin fold, electron transfer protein, metal binding protein, electron transport
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 19168.91

Authors

Abriata, L.A.,Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gkazonis, P.,Spyroulias, G.A.,Vila, A.J.,Wang, S. (deposition date: 2008-07-28, release date: 2008-09-09, Last modification date: 2024-05-22)

Primary citation

Abriata, L.A.,Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gkazonis, P.,Spyroulias, G.A.,Vila, A.J.,Wang, S.
Mechanism of Cu(A) assembly.
Nat.Chem.Biol., 4:599-601, 2008

PubMed Abstract: 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.

PubMed: 18758441
DOI: 10.1038/nchembio.110

Experimental method

SOLUTION NMR