1kmm: Difference between revisions

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-[[Image:1kmm.gif|left|200px]]<br />
-<applet load="1kmm" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1kmm, resolution 2.6&Aring;" />
-'''HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE'''<br />
-==Overview==
+==HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDYL-ADENYLATE==
-The 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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9207058 (full description)]]
+<StructureSection load='1kmm' size='340' side='right'caption='[[1kmm]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1kmm]] is a 4 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=1KMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KMM FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HAM:HISTIDYL-ADENOSINE+MONOPHOSPHATE'>HAM</scene></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=1kmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmm OCA], [https://pdbe.org/1kmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kmm RCSB], [https://www.ebi.ac.uk/pdbsum/1kmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYH_ECOLI SYH_ECOLI]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <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>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1kmm ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-KMM 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 HAM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Sites: S1A, S1B, S1C and S1D. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KMM OCA]].
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9207058 9207058]
 [[Category: Escherichia coli]]
-[[Category: Histidine--tRNA ligase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Arnez JG]]
-[[Category: Arnez, J.G.]]
+[[Category: Francklyn CS]]
-[[Category: Francklyn, C.S.]]
+[[Category: Moras D]]
-[[Category: Moras, D.]]
-[[Category: HAM]]
-[[Category: aminoacyl-trna synthase]]
-[[Category: ligase]]
-[[Category: synthetase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:41:22 2007''