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2fx3

From Proteopedia

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{{Seed}}
 
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[[Image:2fx3.png|left|200px]]
 
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<!--
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==Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set==
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The line below this paragraph, containing "STRUCTURE_2fx3", creates the "Structure Box" on the page.
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<StructureSection load='2fx3' size='340' side='right'caption='[[2fx3]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_2fx3| PDB=2fx3 | SCENE= }}
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<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>
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/2fx3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2fx3" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16552145}}, adds the Publication Abstract to the page
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16552145 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16552145}}
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__TOC__
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</StructureSection>
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Heffron, S E.]]
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[[Category: Heffron SE]]
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[[Category: Jurnak, F.]]
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[[Category: Jurnak F]]
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[[Category: Moeller, R.]]
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[[Category: Moeller R]]
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[[Category: Ef-tu]]
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[[Category: Merohedral twinning]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:28:22 2008''
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Current revision

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

PDB ID 2fx3

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