2f6u: Difference between revisions

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[[Image:2f6u.gif|left|200px]]


{{Structure
==Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with citrate==
|PDB= 2f6u |SIZE=350|CAPTION= <scene name='initialview01'>2f6u</scene>, resolution 1.550&Aring;
<StructureSection load='2f6u' size='340' side='right'caption='[[2f6u]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>
<table><tr><td colspan='2'>[[2f6u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F6U FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
|GENE= pcrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 Archaeoglobus fulgidus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f6u OCA], [https://pdbe.org/2f6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f6u RCSB], [https://www.ebi.ac.uk/pdbsum/2f6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f6u ProSAT]</span></td></tr>
|RELATEDENTRY=[[1viz|1VIZ]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f6u OCA], [http://www.ebi.ac.uk/pdbsum/2f6u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f6u RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/GGGPS_ARCFU GGGPS_ARCFU] Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. To a much lesser extent, is also able to use heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) as the prenyl donor.<ref>PMID:16377641</ref> <ref>PMID:21761520</ref>
 
== Evolutionary Conservation ==
'''Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with citrate'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/2f6u_consurf.spt"</scriptWhenChecked>
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.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
2F6U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F6U OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f6u ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16377641 16377641]
<references/>
__TOC__
</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Geranylgeranylglycerol-phosphate geranylgeranyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Payandeh J]]
[[Category: Payandeh, J.]]
[[Category: archaeal lipid synthesis]]
[[Category: dimer]]
[[Category: non-canonical tim-barrel]]
[[Category: prenyltransferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:58:48 2008''

Latest revision as of 09:21, 14 February 2024

Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase complexed with citrate

2f6u, resolution 1.55Å

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