2f6x

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(New page: 200px<br /><applet load="2f6x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f6x, resolution 2.000&Aring;" /> '''Crystal Structure o...)
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Revision as of 08:16, 21 November 2007


2f6x, resolution 2.000Å

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Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with sn-G1P and MPD

Overview

We report crystal structures of the citrate and sn-glycerol-1-phosphate, (G1P) complexes of (S)-3-O-geranylgeranylglyceryl phosphate synthase from, Archaeoglobus fulgidus (AfGGGPS) at 1.55 and 2.0 A resolution, respectively. AfGGGPS is an enzyme that performs the committed step in, archaeal lipid biosynthesis, and it presents the first triose phosphate, isomerase (TIM)-barrel structure with a prenyltransferase function. Our, studies provide insight into the catalytic mechanism of AfGGGPS and, demonstrate how it selects for the sn-G1P isomer. The replacement of, "Helix 3" by a "strand" in AfGGGPS, a novel modification to the canonical, TIM-barrel fold, suggests a model of enzyme adaptation that involves a, "greasy slide" and a "swinging door." We propose functions for the, homologous PcrB proteins, which are conserved in a subset of pathogenic, bacteria, as either prenyltransferases or being involved in lipoteichoic, acid biosynthesis. Sequence and structural comparisons lead us to, postulate an early evolutionary history for AfGGGPS, which may highlight, its role in the emergence of Archaea.

About this Structure

2F6X is a Single protein structure of sequence from Archaeoglobus fulgidus with 1GP and MPD as ligands. Active as Geranylgeranylglycerol-phosphate geranylgeranyltransferase, with EC number 2.5.1.42 Full crystallographic information is available from OCA.

Reference

The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme., Payandeh J, Fujihashi M, Gillon W, Pai EF, J Biol Chem. 2006 Mar 3;281(9):6070-8. Epub 2005 Dec 23. PMID:16377641

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