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1adj

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[[Image:1adj.gif|left|200px]]
 
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==HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH HISTIDINE==
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The line below this paragraph, containing "STRUCTURE_1adj", creates the "Structure Box" on the page.
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<StructureSection load='1adj' size='340' side='right'caption='[[1adj]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1adj]] is a 4 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=1ADJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADJ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.7&#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=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1adj| PDB=1adj | SCENE= }}
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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=1adj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adj OCA], [https://pdbe.org/1adj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1adj RCSB], [https://www.ebi.ac.uk/pdbsum/1adj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1adj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYH_THET8 SYH_THET8]
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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/ad/1adj_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=1adj ConSurf].
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<div style="clear:both"></div>
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'''HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH HISTIDINE'''
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==See Also==
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure at 2.7 A resolution of histidyl-tRNA synthetase (HisRS) from Thermus thermophilus in complex with its amino acid substrate histidine has been determined. In the crystal asymmetric unit there are two homodimers, each subunit containing 421 amino acid residues. Each monomer of the enzyme consists of three domains: (1) an N-terminal catalytic domain containing a six-stranded antiparallel beta-sheet and the three motifs common to all class II aminoacyl-tRNA synthetases, (2) a 90-residue C-terminal alpha/beta domain which is common to most class IIa synthetases and is probably involved in recognizing the anticodon stem-loop of tRNA(His), and (3) a HisRS-specific alpha-helical domain inserted into the catalytic domain, between motifs II and III. The position of the insertion domain above the catalytic site suggests that it could clamp onto the acceptor stem of the tRNA during aminoacylation. Two HisRS-specific peptides, 259-RGLDYY and 285-GGRYDG, are intimately involved in forming the binding site for the histidine, a molecule of which is found in the active site of each monomer. The structure of HisRS in complex with histidyl adenylate, produced enzymatically in the crystal, has been determined at 3.2 A resolution. This structure shows that the HisRS-specific Arg-259 interacts directly with the alpha-phosphate of the adenylate on the opposite side to the usual conserved motif 2 arginine. Arg-259 thus substitutes for the divalent cation observed in seryl-tRNA synthetase and plays a crucial catalytic role in the mechanism of histidine activation.
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[[Category: Large Structures]]
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==About this Structure==
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1ADJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADJ OCA].
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==Reference==
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Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase., Aberg A, Yaremchuk A, Tukalo M, Rasmussen B, Cusack S, Biochemistry. 1997 Mar 18;36(11):3084-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9115984 9115984]
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[[Category: Histidine--tRNA ligase]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Aberg, A.]]
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[[Category: Aberg A]]
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[[Category: Cusack, S.]]
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[[Category: Cusack S]]
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[[Category: Amino acid]]
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[[Category: Histidine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:07:48 2008''
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Current revision

HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH HISTIDINE

PDB ID 1adj

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