2j1p
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the geranylgeranyl diphosphate synthase from | + | 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 Structure== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Structure and | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17176041 17176041] |
[[Category: Sinapis alba]] | [[Category: Sinapis alba]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Beyer, P.]] | [[Category: Beyer, P.]] | ||
| - | [[Category: Kloer, D | + | [[Category: Kloer, D P.]] |
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: Welsch, R.]] | [[Category: Welsch, R.]] | ||
[[Category: BME]] | [[Category: BME]] | ||
| Line 31: | Line 31: | ||
[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:21 2008'' |
Revision as of 15:58, 21 February 2008
|
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 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 Structure
2J1P is a Single protein structure of sequence from Sinapis alba with , and as ligands. Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 17:58:21 2008
Categories: Sinapis alba | Single protein | Beyer, P. | Kloer, D P. | Schulz, G E. | Welsch, R. | BME | GRG | PGO | Carotenoid biosynthesis | Chloroplast | Geranylgeranyl diphosphate | Isoprene biosynthesis | Isoprenoid diphosphate synthase | Isoprenyl transtransferase | Multifunctional enzyme | Plastid | Transferase | Transit peptide
