5MVO
FoxE P43212 crystal structure of Rhodopseudomonas ferrooxidans SW2 putative iron oxidase
Summary for 5MVO
| Entry DOI | 10.2210/pdb5mvo/pdb |
| Descriptor | FoxE, HEME C, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | cytochrome-c, electron transfer, photoferrotrophy, electron transport |
| Biological source | Rhodobacter sp. SW2 |
| Total number of polymer chains | 3 |
| Total formula weight | 99206.76 |
| Authors | Pereira, L.,Saraiva, I.H.,Oliveira, A.S.,Soares, C.,Gomes, R.O.,Frazao, C. (deposition date: 2017-01-17, release date: 2018-02-28, Last modification date: 2024-01-17) |
| Primary citation | Pereira, L.,Saraiva, I.H.,Coelho, R.,Newman, D.K.,Louro, R.O.,Frazao, C. Crystallization and preliminary crystallographic studies of FoxE from Rhodobacter ferrooxidans SW2, an Fe(II) oxidoreductase involved in photoferrotrophy. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 68:1106-1108, 2012 Cited by PubMed Abstract: FoxE is a protein encoded by the foxEYZ operon of Rhodobacter ferrooxidans SW2 that is involved in Fe(II)-based anoxygenic photosynthesis (`photoferrotrophy'). It is thought to reside in the periplasm, where it stimulates light-dependent Fe(II) oxidation. It contains 259 residues, including two haem c-binding motifs. As no three-dimensional model is available and there is no structure with a similar sequence, crystals of FoxE were produced. They diffracted to 2.44 Å resolution using synchrotron radiation at the Fe edge. The phase problem was solved by SAD using SHELXC/D/E and the experimental maps confirmed the presence of two haems per molecule. PubMed: 22949206DOI: 10.1107/S174430911203271X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.668 Å) |
Structure validation
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