1kmm: Difference between revisions
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==HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE== | ==HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE== | ||
<StructureSection load='1kmm' size='340' side='right' caption='[[1kmm]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1kmm' size='340' side='right' caption='[[1kmm]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HAM:HISTIDYL-ADENOSINE+MONOPHOSPHATE'>HAM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HAM:HISTIDYL-ADENOSINE+MONOPHOSPHATE'>HAM</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21] </span></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=1kmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmm OCA], [http://pdbe.org/1kmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kmm RCSB], [http://www.ebi.ac.uk/pdbsum/1kmm PDBsum]</span></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=1kmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmm OCA], [http://pdbe.org/1kmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kmm RCSB], [http://www.ebi.ac.uk/pdbsum/1kmm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kmm_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/km/1kmm_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1kmm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1kmm" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:38, 25 January 2018
HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATEHISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of an enzyme-substrate complex with histidyl-tRNA synthetase from Escherichia coli, ATP, and the amino acid analog histidinol is described and compared with the previously obtained enzyme-product complex with histidyl-adenylate. An active site arginine, Arg-259, unique to all histidyl-tRNA synthetases, plays the role of the catalytic magnesium ion seen in seryl-tRNA synthetase. When Arg-259 is substituted with histidine, the apparent second order rate constant (kcat/Km) for the pyrophosphate exchange reaction and the aminoacylation reaction decreases 1,000-fold and 500-fold, respectively. Crystals soaked with MnCl2 reveal the existence of two metal binding sites between beta- and gamma-phosphates; these sites appear to stabilize the conformation of the pyrophosphate. The use of both conserved metal ions and arginine in phosphoryl transfer provides evidence of significant early functional divergence of class II aminoacyl-tRNA synthetases. The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase.,Arnez JG, Augustine JG, Moras D, Francklyn CS Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7144-9. PMID:9207058[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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