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1g51

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[[Image:1g51.jpg|left|200px]]<br /><applet load="1g51" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g51, resolution 2.40&Aring;" />
 
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'''ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION'''<br />
 
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==Overview==
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==ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION==
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The crystal structures of Thermus thermophilus aspartyl-tRNA synthetase and of its complex with ATP, Mg2+ and aspartic acid, show in situ formation of the amino acid adenylate and furnish experimental evidence for the modes of recognition of aspartic acid and ATP. The amino acid fits in a predefined specific site in which it replaces water molecules without significant conformational changes of the binding residues. This mode of selection is reminiscent of the lock and key concept. The pocket is closed by the movement of a histidine side chain from a neighbouring loop acting as a valve. ATP binding is driven by the stacking of the adenine upon the otherwise fixed aromatic ring of the class-II-invariant phenylalanine Phe235. Specific recognition is achieved by interactions with the flexible side chains of other class-II-conserved residues. Conformational changes have been identified which allow the description of a reaction pathway including both lock-and-key and induced-fit interactions. This pathway can presumably be extended to all class II aaRS.
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<StructureSection load='1g51' size='340' side='right'caption='[[1g51]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1g51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G51 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]] 2.4&#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=AMO:ASPARTYL-ADENOSINE-5-MONOPHOSPHATE'>AMO</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1g51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g51 OCA], [https://pdbe.org/1g51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g51 RCSB], [https://www.ebi.ac.uk/pdbsum/1g51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g51 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYD_THETH SYD_THETH]
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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/g5/1g51_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=1g51 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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1G51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=AMO:'>AMO</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1G51 OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase., Poterszman A, Delarue M, Thierry JC, Moras D, J Mol Biol. 1994 Nov 25;244(2):158-67. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7966328 7966328]
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[[Category: Large Structures]]
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[[Category: Aspartate--tRNA ligase]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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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: Poterzsman, A.]]
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[[Category: Poterzsman A]]
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[[Category: Thierry, J C.]]
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[[Category: Thierry JC]]
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[[Category: AMO]]
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[[Category: AMP]]
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[[Category: SO4]]
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[[Category: aminoacyl trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:13 2008''
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Current revision

ASPARTYL TRNA SYNTHETASE FROM THERMUS THERMOPHILUS AT 2.4 A RESOLUTION

PDB ID 1g51

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