2IGA
Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.
Summary for 2IGA
| Entry DOI | 10.2210/pdb2iga/pdb |
| Related | 2IG9 |
| Descriptor | Homoprotocatechuate 2,3-dioxygenase, FE (II) ION, CHLORIDE ION, ... (10 entities in total) |
| Functional Keywords | oxygenase, extradiol, fe(ii), homoprotocatechuate, alkylperoxo intermediate, substrate-semiquinone, open-ring product, oxidoreductase |
| Biological source | Brevibacterium fuscum |
| Total number of polymer chains | 4 |
| Total formula weight | 169371.19 |
| Authors | Kovaleva, E.G.,Lipscomb, J.D. (deposition date: 2006-09-22, release date: 2007-04-24, Last modification date: 2023-08-30) |
| Primary citation | Kovaleva, E.G.,Lipscomb, J.D. Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates Science, 316:453-457, 2007 Cited by PubMed Abstract: We report the structures of three intermediates in the O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family. PubMed: 17446402DOI: 10.1126/science.1134697 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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