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1efu

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[[Image:1efu.jpg|left|200px]]<br /><applet load="1efu" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1efu, resolution 2.5&Aring;" />
 
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'''ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI==
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The crystal structure of the EF-Tu.EF-Ts complex from Escherichia coli has, been determined to a resolution of 2.5 A. The complex contains two, subunits of each of the elongation factors. The two EF-Ts molecules form a, tight dimer, but there is little contact between the two EF-Tu molecules., The interaction of EF-Ts with EF-Tu results principally in the disruption, of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for, guanine nucleotides.
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<StructureSection load='1efu' size='340' side='right'caption='[[1efu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1efu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The September 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Elongation Factors'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_9 10.2210/rcsb_pdb/mom_2006_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EFU FirstGlance]. <br>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1efu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efu OCA], [https://pdbe.org/1efu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1efu RCSB], [https://www.ebi.ac.uk/pdbsum/1efu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1efu 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/ef/1efu_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=1efu ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EFU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1EFU with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFU OCA].
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*[[Elongation factor|Elongation factor]]
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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==Reference==
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__TOC__
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The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution., Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R, Nature. 1996 Feb 8;379(6565):511-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8596629 8596629]
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</StructureSection>
[[Category: Elongation Factors]]
[[Category: Elongation Factors]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Berthet-Colominas, C.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Cusack, S.]]
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[[Category: Berthet-Colominas C]]
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[[Category: Kawashima, T.]]
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[[Category: Cusack S]]
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[[Category: Leberman, R.]]
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[[Category: Kawashima T]]
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[[Category: Wulff, M.]]
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[[Category: Leberman R]]
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[[Category: complex (two elongation factors)]]
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[[Category: Wulff M]]
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[[Category: elongation factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:01 2008''
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Current revision

ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI

PDB ID 1efu

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