1a8h

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[[Image:1a8h.gif|left|200px]]
 
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{{Structure
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==METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS==
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|PDB= 1a8h |SIZE=350|CAPTION= <scene name='initialview01'>1a8h</scene>, resolution 2.00&Aring;
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<StructureSection load='1a8h' size='340' side='right'caption='[[1a8h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1a8h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8H FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10]
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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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=1a8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8h OCA], [https://pdbe.org/1a8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8h RCSB], [https://www.ebi.ac.uk/pdbsum/1a8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8h ProSAT], [https://www.topsan.org/Proteins/RSGI/1a8h TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYM_THET8 SYM_THET8] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
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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/a8/1a8h_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=1a8h ConSurf].
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<div style="clear:both"></div>
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'''METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''
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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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Background: The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. The 10 class I synthetases are considered to have in common the catalytic domain structure based on the Rossmann fold, which is totally different from the class II catalytic domain structure. The class I synthetases are further divided into three subclasses, a, b and c, according to sequence homology. No conserved structural features for tRNA recognition by class I synthetases have been established. Results: We determined the crystal structure of the class Ia methionyl-tRNA synthetase (MetRS) at 2.0 A resolution, using MetRS from an extreme thermophile, Thermus thermophilus HB8. The T. thermophilus MetRS structure is in full agreement with the biochemical and genetic data from Escherichia coli MetRS. The conserved 'anticodon-binding' residues are spatially clustered on an alpha-helix-bundle domain. The Rossmann-fold and anticodon-binding domains are connected by a beta-alpha-alpha-beta-alpha topology ('SC fold') domain that contains the class I specific KMSKS motif. Conclusions: The alpha-helix-bundle domain identified in the MetRS structure is the signature of the class Ia enzymes, as it was also identified in the class Ia structures of the isoleucyl- and arginyl-tRNA synthetases. The beta-alpha-alpha-beta-alpha topology domain, which can now be identified in all known structures of the class Ia and Ib synthetases, is likely to dock with the inner side of the L-shaped tRNA, thereby positioning the anticodon stem.
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus HB8]]
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==About this Structure==
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[[Category: Giege R]]
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1A8H 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=1A8H OCA].
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[[Category: Konno M]]
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[[Category: Kuwabara S]]
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==Reference==
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[[Category: Lober B]]
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The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules., Sugiura I, Nureki O, Ugaji-Yoshikawa Y, Kuwabara S, Shimada A, Tateno M, Lorber B, Giege R, Moras D, Yokoyama S, Konno M, Structure. 2000 Feb 15;8(2):197-208. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10673435 10673435]
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[[Category: Moras D]]
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[[Category: Methionine--tRNA ligase]]
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[[Category: Nureki O]]
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[[Category: Single protein]]
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[[Category: Sugiura I]]
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[[Category: Thermus thermophilus]]
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[[Category: Ugaji Y]]
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[[Category: Giege, R.]]
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[[Category: Yokoyama S]]
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[[Category: Konno, M.]]
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[[Category: Kuwabara, S.]]
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[[Category: Lober, B.]]
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[[Category: Moras, D.]]
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[[Category: Nureki, O.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Sugiura, I.]]
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[[Category: Ugaji, Y.]]
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[[Category: Yokoyama, S.]]
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[[Category: ZN]]
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[[Category: aminoacyl-trna synthetase]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rossmann fold]]
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[[Category: rsgi]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:54:23 2008''
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Current revision

METHIONYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

PDB ID 1a8h

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