2J1O
Geranylgeranyl diphosphate synthase from Sinapis alba
Summary for 2J1O
| Entry DOI | 10.2210/pdb2j1o/pdb |
| Related | 2J1P |
| Descriptor | GERANYLGERANYL PYROPHOSPHATE SYNTHETASE, GLYCEROL (3 entities in total) |
| Functional Keywords | transferase, isoprene biosynthesis, multifunctional enzyme, carotenoid biosynthesis, isoprenyl transtransferase, isoprenoid diphosphate synthase, transit peptide, chloroplast |
| Biological source | SINAPIS ALBA (WHITE MUSTARD) |
| Cellular location | Plastid, chloroplast stroma (Probable): Q43133 |
| Total number of polymer chains | 1 |
| Total formula weight | 29021.49 |
| Authors | Kloer, D.P.,Welsch, R.,Beyer, P.,Schulz, G.E. (deposition date: 2006-08-15, release date: 2007-01-02, Last modification date: 2024-05-08) |
| Primary citation | Kloer, D.P.,Welsch, R.,Beyer, P.,Schulz, G.E. Structure and Reaction Geometry of Geranylgeranyl Diphosphate Synthase from Sinapis Alba. Biochemistry, 45:15197-, 2006 Cited by PubMed Abstract: The crystal structure of the geranylgeranyl diphosphate synthase from Sinapis alba (mustard) has been solved in two crystal forms at 1.8 and 2.0 A resolutions. In one of these forms, the dimeric enzyme binds one molecule of the final product geranylgeranyl diphosphate in one subunit. The chainfold of the enzyme corresponds to that of other members of the farnesyl diphosphate synthase family. Whereas the binding modes of the two substrates dimethylallyl diphosphate and isopentenyl diphosphate at the allyl and isopentenyl sites, respectively, have been established with other members of the family, the complex structure presented reveals for the first time the binding mode of a reaction product at the isopentenyl site. The binding geometry of substrates and product in conjunction with the protein environment and the established chemistry of the reaction provide a clear picture of the reaction steps and atom displacements. Moreover, a comparison with a ligated homologous structure outlined an appreciable induced fit: helix alpha8 and its environment undergo a large conformational change when either the substrate dimethylallyl diphosphate or an analogue is bound to the allyl site; only a minor conformational change occurs when the other substrate isopentenyl diphosphate or the product is bound to the isopentenyl site. PubMed: 17176041DOI: 10.1021/BI061572K PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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