1NFV
X-ray structure of Desulfovibrio desulfuricans bacterioferritin: the diiron centre in different catalytic states (as-isolated structure)
1NFV の概要
| エントリーDOI | 10.2210/pdb1nfv/pdb |
| 関連するPDBエントリー | 1NF4 1NF6 |
| 分子名称 | bacterioferritin, FE (III) ION, SULFATE ION, ... (7 entities in total) |
| 機能のキーワード | bacterioferritin, 24 subunits in the active molecule, diiron centre, haem fe-coproporphyrin iii cofactor, iron storage-electron transport complex, iron storage/electron transport |
| 由来する生物種 | Desulfovibrio desulfuricans |
| タンパク質・核酸の鎖数 | 16 |
| 化学式量合計 | 333169.37 |
| 構造登録者 | Macedo, S.,Romao, C.V.,Mitchell, E.,Matias, P.M.,Liu, M.Y.,Xavier, A.V.,LeGall, J.,Teixeira, M.,Lindley, P.,Carrondo, M.A. (登録日: 2002-12-16, 公開日: 2003-04-01, 最終更新日: 2024-12-25) |
| 主引用文献 | Macedo, S.,Romao, C.V.,Mitchell, E.,Matias, P.M.,Liu, M.Y.,Xavier, A.V.,LeGall, J.,Teixeira, M.,Lindley, P.,Carrondo, M.A. The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans NAT.STRUCT.BIOL., 10:285-290, 2003 Cited by PubMed Abstract: The first crystal structure of a native di-iron center in an iron-storage protein (bacterio)ferritin is reported. The protein, isolated from the anaerobic bacterium Desulfovibrio desulfuricans, has the unique property of having Fe-coproporphyrin III as its heme cofactor. The three-dimensional structure of this bacterioferritin was determined in three distinct catalytic/redox states by X-ray crystallography (at 1.95, 2.05 and 2.35 A resolution), corresponding to different intermediates of the di-iron ferroxidase site. Conformational changes associated with these intermediates support the idea of a route for iron entry into the protein shell through a pore that passes through the di-iron center. Molecular surface and electrostatic potential calculations also suggest the presence of another ion channel, distant from the channels at the three- and four-fold axes proposed as points of entry for the iron atoms. PubMed: 12627224DOI: 10.1038/nsb909 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.95 Å) |
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