1dg1

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[[Image:1dg1.gif|left|200px]]
 
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{{Structure
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==WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).==
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|PDB= 1dg1 |SIZE=350|CAPTION= <scene name='initialview01'>1dg1</scene>, resolution 2.50&Aring;
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<StructureSection load='1dg1' size='340' side='right'caption='[[1dg1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
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<table><tr><td colspan='2'>[[1dg1]] is a 2 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=1DG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DG1 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.5&#8491;</td></tr>
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|GENE=
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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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}}
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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=1dg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dg1 OCA], [https://pdbe.org/1dg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dg1 RCSB], [https://www.ebi.ac.uk/pdbsum/1dg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dg1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EFTU2_ECOLI EFTU2_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/dg/1dg1_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=1dg1 ConSurf].
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<div style="clear:both"></div>
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'''WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).'''
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==See Also==
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: The bacterial elongation factor EF-Tu recognizes and transports aminoacyl-tRNAs to mRNA-programmed ribosomes. EF-Tu shares many structural and functional properties with other GTPases whose conformations are regulated by guanine nucleotides. RESULTS: An intact form of Escherichia coli EF-Tu complexed with GDP has been crystallized in the presence of the EF-Tu-specific antibiotic GE2270 A. The three-dimensional structure has been solved by X-ray diffraction analysis and refined to a final crystallographic R factor of 17.2% at a resolution of 2.5 A. The location of the GE2270 A antibiotic-binding site could not be identified. CONCLUSIONS: The structure of EF-Tu-GDP is nearly identical to that of a trypsin-modified form of EF-Tu-GDP, demonstrating conclusively that the protease treatment had not altered any essential structural features. The present structure represents the first view of an ordered Switch I region in EF-Tu-GDP and reveals similarities with two other GTPases complexed with GDP: Ran and ADP-ribosylation factor-1. A comparison of the Switch I regions of the GTP and GDP forms of EF-Tu also reveals that a segment, six amino acids in length, completely converts from an alpha helix in the GTP complex to beta secondary structure in the GDP form. The alpha to beta switch in EF-Tu may represent a prototypical activation mechanism for other protein families.
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==About this Structure==
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1DG1 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=1DG1 OCA].
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==Reference==
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An alpha to beta conformational switch in EF-Tu., Abel K, Yoder MD, Hilgenfeld R, Jurnak F, Structure. 1996 Oct 15;4(10):1153-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8939740 8939740]
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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: Abel, K.]]
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[[Category: Abel K]]
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[[Category: Hilgenfeld, R.]]
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[[Category: Hilgenfeld R]]
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[[Category: Jurnak, F.]]
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[[Category: Jurnak F]]
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[[Category: Yoder, M.]]
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[[Category: Yoder M]]
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[[Category: GDP]]
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[[Category: MG]]
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[[Category: alpha beta shift]]
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[[Category: elongation factor]]
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[[Category: gdp binding]]
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[[Category: gtpase]]
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[[Category: trna binding]]
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[[Category: ts binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:30:26 2008''
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Current revision

WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).

PDB ID 1dg1

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