3vzz
Crystal structure of PcrB complexed with FsPP from bacillus subtilis subap. subtilis str. 168
Structural highlights
FunctionPCRB_BACSU Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Can not use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor.[1] [2] [3] Publication Abstract from PubMedWell structured: As a new triose phosphate isomerase (TIM) barrel-fold prenyl transferase, PcrB catalyzes the production of heptaprenylglyceryl phosphate from heptaprenyl diphosphate and glycerol-1-phosphate. Crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus in complex with ligands were solved, and together with site-directed mutagenesis and bioinformatics analyses, clearly reveal the catalytic mechanism of the enzyme. Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus.,Ren F, Feng X, Ko TP, Huang CH, Hu Y, Chan HC, Liu YL, Wang K, Chen CC, Pang X, He M, Li Y, Oldfield E, Guo RT Chembiochem. 2013 Jan 21;14(2):195-9. doi: 10.1002/cbic.201200748. Epub 2013 Jan , 15. PMID:23322418[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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