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1ady

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(New page: 200px<br /><applet load="1ady" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ady, resolution 2.8&Aring;" /> '''HISTIDYL-TRNA SYNTHET...)
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[[Image:1ady.gif|left|200px]]<br /><applet load="1ady" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ady, resolution 2.8&Aring;" />
 
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'''HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH HISTIDYL-ADENYLATE'''<br />
 
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==Overview==
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==HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH HISTIDYL-ADENYLATE==
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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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<StructureSection load='1ady' size='340' side='right'caption='[[1ady]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ady]] 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=1ADY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADY 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]] 2.8&#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=HAM:HISTIDYL-ADENOSINE+MONOPHOSPHATE'>HAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1ady FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ady OCA], [https://pdbe.org/1ady PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ady RCSB], [https://www.ebi.ac.uk/pdbsum/1ady PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ady 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/1ady_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=1ady 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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1ADY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with SO4 and HAM as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ADY 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 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9115984 9115984]
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[[Category: Large Structures]]
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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: HAM]]
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[[Category: SO4]]
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[[Category: amino acid]]
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[[Category: histidyl-adenylate]]
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[[Category: trna synthetase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:47:06 2007''
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Current revision

HISTIDYL-TRNA SYNTHETASE IN COMPLEX WITH HISTIDYL-ADENYLATE

PDB ID 1ady

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