2j1o: Difference between revisions
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Revision as of 18:17, 30 October 2007
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GERANYLGERANYL DIPHOSPHATE SYNTHASE FROM SINAPIS ALBA
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 ... [(full description)]
About this StructureAbout this Structure
2J1O is a [Single protein] structure of sequence from [Sinapis alba] with GOL as [ligand]. Structure known Active Site: AC1. 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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