2j1o
GERANYLGERANYL DIPHOSPHATE SYNTHASE FROM SINAPIS ALBA
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OverviewOverview
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.
About this StructureAbout this Structure
2J1O is a Single protein structure of sequence from Sinapis alba with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structure and Reaction Geometry of Geranylgeranyl Diphosphate Synthase from Sinapis alba(,)., Kloer DP, Welsch R, Beyer P, Schulz GE, Biochemistry. 2006 Dec 26;45(51):15197-204. Epub 2006 Dec 1. PMID:17176041
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