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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[[Image:2f6x.gif|left|200px]]<br /><applet load="2f6x" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="2f6x, resolution 2.000&Aring;" />
'''Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with sn-G1P and MPD'''<br />
'''Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with sn-G1P and MPD'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2F6X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with 1GP and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Geranylgeranylglycerol-phosphate_geranylgeranyltransferase Geranylgeranylglycerol-phosphate geranylgeranyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.42 2.5.1.42] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F6X OCA].
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2F6X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=1GP:'>1GP</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Geranylgeranylglycerol-phosphate_geranylgeranyltransferase Geranylgeranylglycerol-phosphate geranylgeranyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.42 2.5.1.42] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F6X OCA].
==Reference==
==Reference==
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[[Category: Geranylgeranylglycerol-phosphate geranylgeranyltransferase]]
[[Category: Geranylgeranylglycerol-phosphate geranylgeranyltransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Payandeh, J.M.]]
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[[Category: Payandeh, J M.]]
[[Category: 1GP]]
[[Category: 1GP]]
[[Category: MPD]]
[[Category: MPD]]
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[[Category: non-canonical tim-barrel; prenyltransferase; archaeal lipid synthesis; sn-glycerol-1-phosphate; 2-methyl-2]]
[[Category: non-canonical tim-barrel; prenyltransferase; archaeal lipid synthesis; sn-glycerol-1-phosphate; 2-methyl-2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:24:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:18:20 2008''

Revision as of 15:18, 21 February 2008


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 and 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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