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| [[Image:1htt.gif|left|200px]]
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| {{Structure
| | ==HISTIDYL-TRNA SYNTHETASE== |
| |PDB= 1htt |SIZE=350|CAPTION= <scene name='initialview01'>1htt</scene>, resolution 2.6Å
| | <StructureSection load='1htt' size='340' side='right'caption='[[1htt]], [[Resolution|resolution]] 2.60Å' scene=''> |
| |SITE= <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>
| | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>
| | <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> |
| |ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| |GENE=
| | <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> |
| |DOMAIN=
| | <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> |
| |RELATEDENTRY=
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1htt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htt OCA], [http://www.ebi.ac.uk/pdbsum/1htt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1htt RCSB]</span>
| | == 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/ht/1htt_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=1htt ConSurf]. |
| | <div style="clear:both"></div> |
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| '''HISTIDYL-TRNA SYNTHETASE'''
| | ==See Also== |
| | | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| 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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| ==About this Structure==
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| 1HTT is a [[Single protein]] structure of sequence from [http://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].
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| ==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/7556055 7556055]
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| [[Category: Escherichia coli]] | | [[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: Harris DC]] |
| [[Category: Harris, D C.]] | | [[Category: Mitschler A]] |
| [[Category: Mitschler, A.]] | | [[Category: Moras D]] |
| [[Category: Moras, D.]] | | [[Category: Rees B]] |
| [[Category: Rees, B.]] | |
| [[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 Mar 30 21:10:19 2008''
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