1htt

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[[Image:1htt.gif|left|200px]]<br /><applet load="1htt" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1htt, resolution 2.6&Aring;" />
 
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'''HISTIDYL-TRNA SYNTHETASE'''<br />
 
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==Overview==
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==HISTIDYL-TRNA SYNTHETASE==
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The crystal structure at 2.6 A of the histidyl-tRNA synthetase from, Escherichia coli complexed with histidyl-adenylate has been determined., The enzyme is a homodimer with a molecular weight of 94 kDa and belongs to, the class II of aminoacyl-tRNA synthetases (aaRS). The asymmetric unit is, composed of two homodimers. Each monomer consists of two domains. The, N-terminal catalytic core domain contains a six-stranded antiparallel, beta-sheet sitting on two alpha-helices, which can be superposed with the, catalytic domains of yeast AspRS, and GlyRS and SerRS from Thermus, thermophilus with a root-mean-square difference on the C alpha atoms of, 1.7-1.9 A. The active sites of all four monomers are occupied by, histidyl-adenylate, which apparently forms during crystallization. The 100, residue C-terminal alpha/beta domain resembles half of a beta-barrel, and, provides an independent domain oriented to contact the anticodon stem and, part of the anticodon loop of tRNA(His). The modular domain organization, of histidyl-tRNA synthetase reiterates a repeated theme in aaRS, and its, structure should provide insight into the ability of certain aaRS to, aminoacylate minihelices and other non-tRNA molecules.
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<StructureSection load='1htt' size='340' side='right'caption='[[1htt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1htt]] 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=1HTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTT 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]] 2.6&#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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</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=1htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htt OCA], [https://pdbe.org/1htt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htt RCSB], [https://www.ebi.ac.uk/pdbsum/1htt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYH_ECOLI SYH_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/ht/1htt_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=1htt 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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1HTT 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 <scene name='pdbligand=AMP:'>AMP</scene> 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] Known structural/functional Sites: <scene name='pdbsite=S1A:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1A</scene>, <scene name='pdbsite=S1B:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1B</scene>, <scene name='pdbsite=S1C:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1C</scene> and <scene name='pdbsite=S1D:HIS+And+Atp+Binding+Sites,+Product+Of+First+Reaction+(In+...'>S1D</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTT 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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Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate., Arnez JG, Harris DC, Mitschler A, Rees B, Francklyn CS, Moras D, EMBO J. 1995 Sep 1;14(17):4143-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7556055 7556055]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Histidine--tRNA ligase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Arnez JG]]
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[[Category: Arnez, J.G.]]
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[[Category: Francklyn CS]]
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[[Category: Francklyn, C.S.]]
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[[Category: Harris DC]]
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[[Category: Harris, D.C.]]
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[[Category: Mitschler A]]
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[[Category: Mitschler, A.]]
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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: AMP]]
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[[Category: aminoacyl-trna synthase]]
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[[Category: complex (trna synthetase/his-adenylate)]]
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[[Category: ligase]]
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[[Category: synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:50:16 2008''
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Current revision

HISTIDYL-TRNA SYNTHETASE

PDB ID 1htt

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