2AJ0
Solution structure of apoCadA
2AJ0 の概要
| エントリーDOI | 10.2210/pdb2aj0/pdb |
| 関連するPDBエントリー | 2AJ1 |
| NMR情報 | BMRB: 6811 |
| 分子名称 | Probable cadmium-transporting ATPase (1 entity in total) |
| 機能のキーワード | ferrodoxin-like fold, beta-alpha-beta-beta-alpha-beta, metal binding protein, hydrolase |
| 由来する生物種 | Listeria monocytogenes |
| 細胞内の位置 | Cell membrane; Multi-pass membrane protein: Q60048 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 7708.73 |
| 構造登録者 | Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Su, X.-C.,Miras, R.,Bal, N.,Mintz, E.,Catty, P.,Shokes, J.E.,Scott, R.A. (登録日: 2005-08-01, 公開日: 2006-05-02, 最終更新日: 2024-05-29) |
| 主引用文献 | Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Su, X.-C.,Miras, R.,Bal, N.,Mintz, E.,Catty, P.,Shokes, J.E.,Scott, R.A. Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA J.Mol.Biol., 356:638-650, 2006 Cited by PubMed Abstract: In bacteria, P1-type ATPases are responsible for resistance to di- and monovalent toxic heavy metals by taking them out of the cell. These ATPases have a cytoplasmic N terminus comprising metal binding domains defined by a betaalphabetabetaalphabeta fold and a CXXC metal binding motif. To check how the structural properties of the metal binding site in the N terminus can influence the metal specificity of the ATPase, the first structure of a Cd(II)-ATPase N terminus was determined by NMR and its coordination sphere was investigated by X-ray absorption spectroscopy. A novel metal binding environment was found, comprising the two conserved Cys residues of the metal binding motif and a Glu in loop 5. A bioinformatic search identifies an ensemble of highly homologous sequences presumably with the same function. Another group of highly homologous sequences is found which can be referred to as zinc-detoxifying P1-type ATPases with the metal binding pattern DCXXC in the N terminus. Because no carboxylate groups participate in Cu(I) or Ag(I) binding sites, we suggest that the acidic residue plays a key role in the coordination properties of divalent cations, hence conferring a function to the N terminus in the metal specificity of the ATPase. PubMed: 16388822DOI: 10.1016/j.jmb.2005.11.055 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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