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2hcj

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(New page: 200px<br /><applet load="2hcj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hcj, resolution 2.12&Aring;" /> '''"Trypsin-modified El...)
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[[Image:2hcj.jpg|left|200px]]<br /><applet load="2hcj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hcj, resolution 2.12&Aring;" />
 
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'''"Trypsin-modified Elongation Factor Tu in complex with tetracycline"'''<br />
 
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==Overview==
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==Trypsin-modified Elongation Factor Tu in complex with tetracycline==
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Two crystal forms of a complex between trypsin-modified elongation factor, Tu-MgGDP from Escherichia coli and the antibiotic tetracycline have been, solved by X-ray diffraction analysis to resolutions of 2.8 and 2.1 A, respectively. In the P2(1) form, cocrystals were grown from a solution, mixture of the protein and tetracycline. Six copies of the, trypsin-modified EF-Tu-MgGDP-tetracycline complex are arranged as three, sets of dimers in the asymmetric unit. In the second crystal form, tetracycline was diffused into P4(3)2(1)2 crystals, resulting in a, monomeric complex in the asymmetric unit. Atomic coordinates have been, refined to crystallographic R factors of 18.0% for the P2(1) form and, 20.0% for the P4(3)2(1)2 form. In both complexes, tetracycline makes, significant interactions with the GTPase active site of EF-Tu. The, phenoldiketone moiety of tetracycline interacts directly with the Mg(2+), the alpha-phosphate group of GDP and two amino acids, Thr25 and Asp80, which are conserved in the GX(4)GKS/T and DX(2)G sequence motifs found in, all GTPases and many ATPases. The molecular complementarity, previously, unrecognized between invariant groups present in all GTPase/ATPases and, the active moiety of tetracycline, may have wide-ranging implications for, all drugs containing the phenoldiketone moiety as well as for the design, of new compounds targeted against a broad range of GTPases or ATPases.
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<StructureSection load='2hcj' size='340' side='right'caption='[[2hcj]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hcj]] 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=2HCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HCJ 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]] 2.12&#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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TAC:TETRACYCLINE'>TAC</scene></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=2hcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcj OCA], [https://pdbe.org/2hcj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hcj RCSB], [https://www.ebi.ac.uk/pdbsum/2hcj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hcj 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/hc/2hcj_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=2hcj 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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2HCJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, NA, SO4, TAC, GDP and GLV as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HCJ OCA].
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu., Heffron SE, Mui S, Aorora A, Abel K, Bergmann E, Jurnak F, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1392-400. Epub, 2006 Oct 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17057344 17057344]
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[[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: Abel, K.]]
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[[Category: Abel K]]
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[[Category: Aorora, A.]]
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[[Category: Aorora A]]
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[[Category: Bergmann, E.]]
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[[Category: Bergmann E]]
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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: Mui, S.]]
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[[Category: Mui S]]
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[[Category: GDP]]
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[[Category: GLV]]
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[[Category: MG]]
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[[Category: NA]]
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[[Category: SO4]]
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[[Category: TAC]]
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[[Category: complex with tetracycline]]
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[[Category: gtpase center]]
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[[Category: trypsin-modified ef-tu]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:40:18 2007''
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Current revision

Trypsin-modified Elongation Factor Tu in complex with tetracycline

PDB ID 2hcj

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