1eqr

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[[Image:1eqr.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI==
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The line below this paragraph, containing "STRUCTURE_1eqr", creates the "Structure Box" on the page.
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<StructureSection load='1eqr' size='340' side='right'caption='[[1eqr]], [[Resolution|resolution]] 2.70&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'>[[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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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]] 2.7&#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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{{STRUCTURE_1eqr| PDB=1eqr | 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=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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'''CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI'''
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==See Also==
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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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==Overview==
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__TOC__
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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>
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==About this Structure==
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1EQR 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=1EQR OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/10873442 10873442]
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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: Anti-parallel beta strand]]
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[[Category: Beta barrel]]
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[[Category: Domain]]
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[[Category: Oligomer binding fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:25:09 2008''
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Current revision

CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI

PDB ID 1eqr

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