2K6Y

Solution structures of apo form PCuA (cis conformation of the peptide bond involving the nitrogen of P14)

Summary for 2K6Y

Entry DOI	10.2210/pdb2k6y/pdb
Related	2K6V 2K70 2k6w 2k6z
Descriptor	Putative uncharacterized protein TTHA1943 (1 entity in total)
Functional Keywords	pcua, copper transfer protein, cis conformation, metal transport
Biological source	Thermus thermophilus
Total number of polymer chains	1
Total formula weight	13222.55
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 Cited by 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 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation