3SXQ
Structure of a hexameric multiheme c nitrite reductase from the extremophile bacterium Thiolkalivibrio paradoxus
Summary for 3SXQ
| Entry DOI | 10.2210/pdb3sxq/pdb |
| Related | 2OT4 |
| Descriptor | Eight-heme nitrite reductase, HEME C, CALCIUM ION, ... (9 entities in total) |
| Functional Keywords | eight hemes c, nitrite reductase, oxidoreductase |
| Biological source | Thioalkalivibrio paradoxus |
| Total number of polymer chains | 2 |
| Total formula weight | 129907.76 |
| Authors | Polyakov, K.M.,Trofimov, A.A.,Tikhonova, T.V.,Tikhonov, A.V.,Boyko, K.M.,Popov, V.O. (deposition date: 2011-07-15, release date: 2012-09-26, Last modification date: 2024-11-06) |
| Primary citation | Tikhonova, T.,Tikhonov, A.,Trofimov, A.,Polyakov, K.,Boyko, K.,Cherkashin, E.,Rakitina, T.,Sorokin, D.,Popov, V. Comparative structural and functional analysis of two octaheme nitrite reductases from closely related Thioalkalivibrio species. Febs J., 279:4052-4061, 2012 Cited by PubMed Abstract: Octaheme nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio paradoxus was isolated and characterized. A comparative structural and functional analysis of two homologous octaheme nitrite reductases from closely related Thioalkalivibrio species was performed. It was shown that both enzymes have similar catalytic properties, owing to high structural similarity. Both enzymes are characterized by specific structural features distinguishing them from pentaheme cytochrome c nitrite reductases, such as the Tyr-Cys bond in the active site, the hexameric structure resulting in the formation of a void space inside the hexamer, and the product channel that opens into the void interior space of the hexamer. It is suggested that these specific structural features are responsible for the higher nitrite reductase activity, the greater preference for nitrite than for sulfite as a substrate, and the wider pH range of the catalytic activity of octaheme nitrite reductases than of pentaheme homologs. PubMed: 22935005DOI: 10.1111/j.1742-4658.2012.08811.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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