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2hcj

From Proteopedia

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[[Image:2hcj.jpg|left|200px]]
 
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==Trypsin-modified Elongation Factor Tu in complex with tetracycline==
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The line below this paragraph, containing "STRUCTURE_2hcj", creates the "Structure Box" on the page.
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<StructureSection load='2hcj' size='340' side='right'caption='[[2hcj]], [[Resolution|resolution]] 2.12&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'>[[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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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]] 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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{{STRUCTURE_2hcj| PDB=2hcj | 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=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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'''"Trypsin-modified Elongation Factor Tu in complex with tetracycline"'''
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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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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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==About this Structure==
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2HCJ is a [[Protein complex]] structure of sequences 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=2HCJ OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/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: 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://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:07:29 2008''
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Current revision

Trypsin-modified Elongation Factor Tu in complex with tetracycline

PDB ID 2hcj

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