1g51: Difference between revisions

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 <StructureSection load='1g51' size='340' side='right'caption='[[1g51]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1g51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G51 FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</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>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g51 OCA], [http://pdbe.org/1g51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g51 RCSB], [http://www.ebi.ac.uk/pdbsum/1g51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g51 ProSAT]</span></td></tr>
+<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>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYD_THETH SYD_THETH]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:7966328<ref>PMID:7966328</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1g51" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
-[[Category: Aspartate--tRNA ligase]]
 [[Category: Large Structures]]
-[[Category: Delarue, M]]
+[[Category: Thermus thermophilus]]
-[[Category: Moras, D]]
+[[Category: Delarue M]]
-[[Category: Poterzsman, A]]
+[[Category: Moras D]]
-[[Category: Thierry, J C]]
+[[Category: Poterzsman A]]
-[[Category: Aminoacyl trna synthetase]]
+[[Category: Thierry JC]]
-[[Category: Ligase]]