Structural highlights
Function
[GGGPS_ARCFU] Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. To a much lesser extent, is also able to use heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) as the prenyl donor.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We report crystal structures of the citrate and sn-glycerol-1-phosphate (G1P) complexes of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Archaeoglobus fulgidus (AfGGGPS) at 1.55 and 2.0 A resolution, respectively. AfGGGPS is an enzyme that performs the committed step in archaeal lipid biosynthesis, and it presents the first triose phosphate isomerase (TIM)-barrel structure with a prenyltransferase function. Our studies provide insight into the catalytic mechanism of AfGGGPS and demonstrate how it selects for the sn-G1P isomer. The replacement of "Helix 3" by a "strand" in AfGGGPS, a novel modification to the canonical TIM-barrel fold, suggests a model of enzyme adaptation that involves a "greasy slide" and a "swinging door." We propose functions for the homologous PcrB proteins, which are conserved in a subset of pathogenic bacteria, as either prenyltransferases or being involved in lipoteichoic acid biosynthesis. Sequence and structural comparisons lead us to postulate an early evolutionary history for AfGGGPS, which may highlight its role in the emergence of Archaea.
The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme.,Payandeh J, Fujihashi M, Gillon W, Pai EF J Biol Chem. 2006 Mar 3;281(9):6070-8. Epub 2005 Dec 23. PMID:16377641[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Payandeh J, Fujihashi M, Gillon W, Pai EF. The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme. J Biol Chem. 2006 Mar 3;281(9):6070-8. Epub 2005 Dec 23. PMID:16377641 doi:10.1074/jbc.M509377200
- ↑ Guldan H, Matysik FM, Bocola M, Sterner R, Babinger P. Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria. Angew Chem Int Ed Engl. 2011 Aug 22;50(35):8188-91. doi: 10.1002/anie.201101832. , Epub 2011 Jul 14. PMID:21761520 doi:10.1002/anie.201101832
- ↑ Payandeh J, Fujihashi M, Gillon W, Pai EF. The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme. J Biol Chem. 2006 Mar 3;281(9):6070-8. Epub 2005 Dec 23. PMID:16377641 doi:10.1074/jbc.M509377200
