6jo3 | pdb_00006jo3

Crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Thermoplasma acidophilum in complex with substrate sn-glycerol-1-phosphate

spinqualitylabelsall models 6jo3, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jo3 is a 1 chain structure with sequence from Thermoplasma acidophilum DSM 1728. This structure supersedes the now removed PDB entry 5b69. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: 1GP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GGGPS_THEAC 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. Cannot use sn-glycerol-3-phosphate (G3P) as substrate. Publication Abstract from PubMed (S)-3-O-Geranylgeranylglyceryl phosphate synthase (GGGPS) catalyzes the initial ether-bond formation between sn-glycerol 1-phosphate (G1P) and geranylgeranyl pyrophosphate to synthesize (S)-3-O-geranylgeranylglyceryl phosphate in the production of an archaeal cell-membrane lipid molecule. Archaeal GGGPS proteins are divided into two groups (group I and group II). In this study, the crystal structure of the archaeal group II GGGPS from Thermoplasma acidophilum (TaGGGPS) was determined at 2.35 A resolution. The structure of TaGGGPS showed that it has a TIM-barrel fold, the third helix of which is disordered (alpha3*), and that it forms a homodimer, although a pre-existing structure of an archaeal group II GGGPS (from Methanothermobacter thermautotrophicus) showed a hexameric form. The structure of TaGGGPS showed the precise G1P-recognition mechanism of an archaeal group II GGGPS. The structure of TaGGGPS and molecular-dynamics simulation analysis showed fluctuation of the beta2-alpha2, alpha3* and alpha5a regions, which is predicted to be important for substrate uptake and/or product release by TaGGGPS. Crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Thermoplasma acidophilum in complex with the substrate sn-glycerol 1-phosphate.,Nemoto N, Miyazono KI, Tanokura M, Yamagishi A Acta Crystallogr F Struct Biol Commun. 2019 Jul 1;75(Pt 7):470-479. doi:, 10.1107/S2053230X19007453. Epub 2019 Jun 17. PMID:31282866 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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