Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase
作者： M. Fujihashi , Y.-W. Zhang , Y. Higuchi , X.-Y. Li , T. Koyama
关键词: Enzyme 、 Protein structure 、 Prenylation 、 Biochemistry 、 Stereochemistry 、 Binding site 、 Biosynthesis 、 Peptide sequence 、 ATP synthase 、 Transferase 、 Biology
摘要: Undecaprenyl diphosphate synthase (UPS) catalyzes the cis-prenyl chain elongation onto trans, trans-farnesyl (FPP) to produce undecaprenyl (UPP), which is indispensable for biosynthesis of bacterial cell walls. We report here crystal structure UPS as only three-dimensional among elongating enzymes. The classified into a protein fold family and completely different from so-called “isoprenoid fold” that believed be common enzymes relating isoprenoid biosynthesis. Conserved amino acid residues are located around large hydrophobic cleft in structure. A structural P-loop motif, frequently appears various kinds phosphate binding site, found at entrance this cleft. catalytic site determined on basis these features, possible reaction mechanism proposed.
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