1v7u
From Proteopedia
|
Crystal structure of Undecaprenyl Pyrophosphate Synthase with farnesyl pyrophosphate
Overview
Undecaprenyl pyrophosphate synthase (UPPs) catalyzes eight consecutive, condensation reactions of farnesyl pyrophosphate (FPP) with isopentenyl, pyrophosphate (IPP) to form a 55-carbon long-chain product. We previously, reported the crystal structure of the apo-enzyme from Escherichia coli and, the structure of UPPs in complex with sulfate ions (resembling, pyrophosphate of substrate), Mg(2+), and two Triton molecules, (product-like). In the present study, FPP substrate was soaked into the, UPPs crystals, and the complex structure was solved. Based on the crystal, structure, the pyrophosphate head group of FPP is bound to the backbone, NHs of Gly29 and Arg30 as well as the side chains of Asn28, Arg30, and, Arg39 through hydrogen bonds. His43 is close to the C2 carbon of FPP and, may stabilize the farnesyl cation intermediate during catalysis. The, hydrocarbon moiety of FPP is bound with hydrophobic amino acids including, Leu85, Leu88, and Phe89, located on the alpha3 helix. The binding mode of, FPP in cis-type UPPs is apparently different from that of trans-type and, many other prenyltransferases which utilize Asprich motifs for substrate, binding via Mg(2+). The new structure provides a plausible mechanism for, the catalysis of UPPs.
About this Structure
1V7U is a Single protein structure of sequence from Escherichia coli with FPP as ligand. Active as Di-trans,poly-cis-decaprenylcistransferase, with EC number 2.5.1.31 Full crystallographic information is available from OCA.
Reference
Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies., Chang SY, Ko TP, Chen AP, Wang AH, Liang PH, Protein Sci. 2004 Apr;13(4):971-8. PMID:15044730
Page seeded by OCA on Wed Nov 21 04:29:58 2007
