4JKN
Mercury Metallated Pseudomonas aeruginosa Azurin at 1.54 A
4JKN の概要
| エントリーDOI | 10.2210/pdb4jkn/pdb |
| 関連するPDBエントリー | 3UGE |
| 分子名称 | Azurin, MERCURY (II) ION, NITRATE ION, ... (5 entities in total) |
| 機能のキーワード | electron transport, mercury metallation |
| 由来する生物種 | Pseudomonas aeruginosa |
| 細胞内の位置 | Periplasm: P00282 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 57380.24 |
| 構造登録者 | Zampino, A.P.,Masters, F.M.,Bladholm, E.L.,Berry, S.B.,Panzner, M.J.,Ziegler, C.J. (登録日: 2013-03-10, 公開日: 2014-02-19, 最終更新日: 2024-11-27) |
| 主引用文献 | Zampino, A.P.,Masters, F.M.,Bladholm, E.L.,Panzner, M.J.,Berry, S.M.,Leeper, T.C.,Ziegler, C.J. Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity. J.Inorg.Biochem., 141:152-160, 2014 Cited by PubMed Abstract: Mercury(II) metallation of Pseudomonas aeruginosa azurin has been characterized structurally and biochemically. The X-ray crystal structure at 1.5Å of mercury(II) metallated azurin confirms the coordination of mercury at the copper binding active site and a second surface site. These findings are further validated by NMR, Matrix-assisted laser desorption/ionization spectrometry (MALDI), and UV-visible spectroscopic methods indicating copper displacement from the wild-type protein. Bioinformatic analysis has identified homologous human protein domains computationally, and compared them to the structure of azurin, providing a model for human mercury interactions. Study of the mercury-azurin adduct, in combination with other known examples of protein-heavy metal interactions, could provide further insight into the chemical mechanisms of toxicological interactions, leading toward a global understanding of the biological speciation of toxic heavy metals. PubMed: 25265377DOI: 10.1016/j.jinorgbio.2014.09.003 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.536 Å) |
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