2j1p

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spinqualitylabelsall models 2j1p, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

GERANYLGERANYL DIPHOSPHATE SYNTHASE FROM SINAPIS ALBA IN COMPLEX WITH GGPP

Overview

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 Structure

2J1P is a [Single protein] structure of sequence from [Sinapis alba] with GRG, PGO and BME as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

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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