1fps
From Proteopedia
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CRYSTAL STRUCTURE OF RECOMBINANT FARNESYL DIPHOSPHATE SYNTHASE AT 2.6 ANGSTROMS RESOLUTION
Overview
The synthesis of farnesyl diphosphate (FPP), a key intermediate in the, isoprenoid biosynthetic pathway required for the synthesis of cholesterol, and in the formation of prenylated proteins, is catalyzed by the enzyme, farnesyl diphosphate synthase (FPS). The crystal structure of avian, recombinant FPS, the first three-dimensional structure for any, prenyltransferase, was determined to 2.6-A resolution. The enzyme exhibits, a novel fold composed entirely of alpha-helices joined by connecting, loops. The enzyme's most prominent structural feature is the arrangement, of 10 core helices around a large central cavity. Two aspartate-rich, sequences that are highly conserved among the isoprenyl diphosphate, synthase family of prenyltransferases, and are essential for enzymatic, activity, were found on opposite walls of this cavity, with the aspartate, side chains approximately 12 A apart and facing each other. The location, and metal ion binding properties of these sequences suggest that the, conserved aspartate residues participate in substrate binding of, catalysis.
About this Structure
1FPS is a Single protein structure of sequence from Gallus gallus. Active as Geranyltranstransferase, with EC number 2.5.1.10 Full crystallographic information is available from OCA.
Reference
Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution., Tarshis LC, Yan M, Poulter CD, Sacchettini JC, Biochemistry. 1994 Sep 13;33(36):10871-7. PMID:8086404
Page seeded by OCA on Tue Nov 20 15:08:07 2007
