2K6Y
Solution structures of apo form PCuA (cis conformation of the peptide bond involving the nitrogen of P14)
2K6Y の概要
| エントリーDOI | 10.2210/pdb2k6y/pdb |
| 関連するPDBエントリー | 2K6V 2K70 2k6w 2k6z |
| 分子名称 | Putative uncharacterized protein TTHA1943 (1 entity in total) |
| 機能のキーワード | pcua, copper transfer protein, cis conformation, metal transport |
| 由来する生物種 | Thermus thermophilus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 13222.55 |
| 構造登録者 | Abriata, L.A.,Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Gkazonis, P.,Spyroulias, G.A.,Vila, A.J.,Wang, S. (登録日: 2008-07-28, 公開日: 2008-09-09, 最終更新日: 2024-05-22) |
| 主引用文献 | 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: 18758441DOI: 10.1038/nchembio.110 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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