2BIW
Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, native enzyme
Summary for 2BIW
| Entry DOI | 10.2210/pdb2biw/pdb |
| Related | 2BIX |
| Descriptor | APOCAROTENOID-CLEAVING OXYGENASE, (3R)-3-HYDROXY-8'-APOCAROTENOL, FE (III) ION, ... (4 entities in total) |
| Functional Keywords | oxygenase, non-heme iron, carotenoid cleavage, retinal formation, oxidoreductase, dioxygenase |
| Biological source | SYNECHOCYSTIS SP. |
| Total number of polymer chains | 4 |
| Total formula weight | 219338.76 |
| Authors | Kloer, D.P.,Ruch, S.,Al-Babili, S.,Beyer, P.,Schulz, G.E. (deposition date: 2005-01-26, release date: 2005-04-14, Last modification date: 2024-05-01) |
| Primary citation | Kloer, D.P.,Ruch, S.,Al-Babili, S.,Beyer, P.,Schulz, G.E. The Structure of a Retinal-Forming Carotenoid Oxygenase Science, 308:267-, 2005 Cited by PubMed Abstract: Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen. PubMed: 15821095DOI: 10.1126/SCIENCE.1108965 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.39 Å) |
Structure validation
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