1eqr

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(New page: 200px<br /><applet load="1eqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqr, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1eqr.gif|left|200px]]<br /><applet load="1eqr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eqr, resolution 2.70&Aring;" />
 
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'''CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI==
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The crystal structure of aspartyl-tRNA synthetase from Escherichia coli, has been determined to a resolution of 2.7 A. The structure is compared to, the same enzyme co-crystallized with tRNA(Asp) and containing aspartyl, adenylate or ATP. The asymmetric unit contains three monomers of the, enzyme. While most parts of the protein show no significant differences in, the three monomers, a few regions cannot be superimposed. Those regions, are characterized by a high B-factor, and consist mostly of loops that, make contacts with the tRNA in the complexes. The flexibility of the, protein is seen at a global level, by the observation of a 10 to 15, degrees rotation of the N-terminal and insertion domains upon tRNA, binding, and at the level of the individual amino acid residues, by, main-chain and side-chain rearrangements. In contrast to these induced-fit, conformational changes, a few residues essential for the tRNA anticodon or, aspartyl-adenylate recognition exist in a predefined conformation, ensured, by specific interactions within the protein.
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<StructureSection load='1eqr' size='340' side='right'caption='[[1eqr]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eqr]] is a 3 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=1EQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQR 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]] 2.7&#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=MG:MAGNESIUM+ION'>MG</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=1eqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eqr OCA], [https://pdbe.org/1eqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eqr RCSB], [https://www.ebi.ac.uk/pdbsum/1eqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eqr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYD_ECOLI SYD_ECOLI]
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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/eq/1eqr_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=1eqr 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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1EQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EQR OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
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==Reference==
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__TOC__
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Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates., Rees B, Webster G, Delarue M, Boeglin M, Moras D, J Mol Biol. 2000 Jun 23;299(5):1157-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10873442 10873442]
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</StructureSection>
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[[Category: Aspartate--tRNA ligase]]
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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: Boeglin, M.]]
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[[Category: Boeglin M]]
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[[Category: Delarue, M.]]
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[[Category: Delarue M]]
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[[Category: Moras, D.]]
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[[Category: Moras D]]
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[[Category: Rees, B.]]
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[[Category: Rees B]]
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[[Category: Webster, G.]]
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[[Category: Webster G]]
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[[Category: MG]]
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[[Category: anti-parallel beta strand]]
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[[Category: beta barrel]]
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[[Category: domains]]
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[[Category: oligomer binding fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:14:13 2007''
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Current revision

CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI

PDB ID 1eqr

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