1f75
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(New page: 200px<br /><applet load="1f75" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f75, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 12:33, 20 November 2007
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CRYSTAL STRUCTURE OF UNDECAPRENYL DIPHOSPHATE SYNTHASE FROM MICROCOCCUS LUTEUS B-P 26
Overview
Undecaprenyl diphosphate synthase (UPS) catalyzes the cis-prenyl chain, elongation onto trans, trans-farnesyl diphosphate (FPP) to produce, undecaprenyl diphosphate (UPP), which is indispensable for the, biosynthesis of bacterial cell walls. We report here the crystal structure, of UPS as the only three-dimensional structure among cis-prenyl chain, elongating enzymes. The structure is classified into a protein fold family, and is completely different from the so-called "isoprenoid synthase fold", that is believed to be a common structure for the enzymes relating to, isoprenoid biosynthesis. Conserved amino acid residues among cis-prenyl, chain elongating enzymes are located around a large hydrophobic cleft in, the UPS structure. A structural P-loop motif, which frequently appears in, the various kinds of phosphate binding site, is found at the entrance of, this cleft. The catalytic site is determined on the basis of these, structural features, from which a possible reaction mechanism is proposed.
About this Structure
1F75 is a Single protein structure of sequence from Micrococcus luteus with SO4 as ligand. Active as Di-trans,poly-cis-decaprenylcistransferase, with EC number 2.5.1.31 Full crystallographic information is available from OCA.
Reference
Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase., Fujihashi M, Zhang YW, Higuchi Y, Li XY, Koyama T, Miki K, Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4337-42. Epub 2001 Apr 3. PMID:11287651
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