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[[Image:2fx3.gif|left|200px]]
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{{STRUCTURE_2fx3|  PDB=2fx3  |  SCENE=  }}
'''Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set'''


==Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set==
<StructureSection load='2fx3' size='340' side='right'caption='[[2fx3]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fx3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FX3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fx3 OCA], [https://pdbe.org/2fx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fx3 RCSB], [https://www.ebi.ac.uk/pdbsum/2fx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fx3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFTU1_ECOLI EFTU1_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]  May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/2fx3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2fx3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli elongation factor Tu-GDP (EF-Tu-GDP) was crystallized in the presence of novel inhibitors. The only crystals which could be grown were epitaxially as well as merohedrally twinned, highly mosaic and diffracted to a resolution of 3.4 A in space group P3(1)21, with unit-cell parameters a = b = 69.55, c = 169.44 A, alpha = beta = 90, gamma = 120 degrees . To determine whether an inhibitor was present in the crystal, a poor-quality X-ray diffraction data set had to be processed. The three-dimensional structure was ultimately solved and the original question answered. The results also reveal a new type of dimer packing for EF-Tu-GDP.


==Overview==
Solving the structure of Escherichia coli elongation factor Tu using a twinned data set.,Heffron SE, Moeller R, Jurnak F Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):433-8. Epub 2006, Mar 18. PMID:16552145<ref>PMID:16552145</ref>
Escherichia coli elongation factor Tu-GDP (EF-Tu-GDP) was crystallized in the presence of novel inhibitors. The only crystals which could be grown were epitaxially as well as merohedrally twinned, highly mosaic and diffracted to a resolution of 3.4 A in space group P3(1)21, with unit-cell parameters a = b = 69.55, c = 169.44 A, alpha = beta = 90, gamma = 120 degrees . To determine whether an inhibitor was present in the crystal, a poor-quality X-ray diffraction data set had to be processed. The three-dimensional structure was ultimately solved and the original question answered. The results also reveal a new type of dimer packing for EF-Tu-GDP.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2FX3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FX3 OCA].
</div>
<div class="pdbe-citations 2fx3" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Solving the structure of Escherichia coli elongation factor Tu using a twinned data set., Heffron SE, Moeller R, Jurnak F, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):433-8. Epub 2006, Mar 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16552145 16552145]
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Heffron, S E.]]
[[Category: Heffron SE]]
[[Category: Jurnak, F.]]
[[Category: Jurnak F]]
[[Category: Moeller, R.]]
[[Category: Moeller R]]
[[Category: Ef-tu]]
[[Category: Merohedral twinning]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:24:23 2008''

Latest revision as of 09:32, 30 August 2023

Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set

2fx3, resolution 3.40Å

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