4AM4
Bacterioferritin from Blastochloris viridis
4AM4 の概要
| エントリーDOI | 10.2210/pdb4am4/pdb |
| 関連するPDBエントリー | 4AM2 4AM4 |
| 分子名称 | BACTERIOFERRITIN, PROTOPORPHYRIN IX CONTAINING FE, FE (III) ION, ... (4 entities in total) |
| 機能のキーワード | metal binding protein, ferroxidase centre, iron storage, di iron centre, double-soaked, iron channel, heme binding |
| 由来する生物種 | BLASTOCHLORIS VIRIDIS |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 37621.34 |
| 構造登録者 | Wahlgren, W.Y.,Omran, H.,von Stetten, D.,Royant, A.,van der Post, S.,Katona, G. (登録日: 2012-03-07, 公開日: 2012-10-31, 最終更新日: 2023-12-20) |
| 主引用文献 | Wahlgren, W.Y.,Omran, H.,von Stetten, D.,Royant, A.,van der Post, S.,Katona, G. Structural Characterization of Bacterioferritin from Blastochloris Viridis. Plos One, 7:46992-, 2012 Cited by PubMed Abstract: Iron storage and elimination of toxic ferrous iron are the responsibility of bacterioferritins in bacterial species. Bacterioferritins are capable of oxidizing iron using molecular oxygen and import iron ions into the large central cavity of the protein, where they are stored in a mineralized form. We isolated, crystallized bacterioferritin from the microaerophilic/anaerobic, purple non-sulfur bacterium Blastochloris viridis and determined its amino acid sequence and X-ray structure. The structure and sequence revealed similarity to other purple bacterial species with substantial differences in the pore regions. Static 3- and 4-fold pores do not allow the passage of iron ions even though structural dynamics may assist the iron gating. On the other hand the B-pore is open to water and larger ions in its native state. In order to study the mechanism of iron import, multiple soaking experiments were performed. Upon Fe(II) and urea treatment the ferroxidase site undergoes reorganization as seen in bacterioferritin from Escherichia coli and Pseudomonas aeruginosa. When soaking with Fe(II) only, a closely bound small molecular ligand is observed close to Fe(1) and the coordination of Glu94 to Fe(2) changes from bidentate to monodentate. DFT calculations indicate that the bound ligand is most likely a water or a hydroxide molecule representing a product complex. On the other hand the different soaking treatments did not modify the conformation of other pore regions. PubMed: 23056552DOI: 10.1371/JOURNAL.PONE.0046992 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.68 Å) |
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