1ati

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[[Image:1ati.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS==
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|PDB= 1ati |SIZE=350|CAPTION= <scene name='initialview01'>1ati</scene>, resolution 2.75&Aring;
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<StructureSection load='1ati' size='340' side='right'caption='[[1ati]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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|SITE= <scene name='pdbsite=SA1:These+Residues+Are+Found+To+Be+Responsible+For+On+The+Ba+...'>SA1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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<table><tr><td colspan='2'>[[1ati]] is a 4 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=1ATI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATI FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine--tRNA_ligase Glycine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.14 6.1.1.14] </span>
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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]] 2.75&#8491;</td></tr>
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|GENE=
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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=1ati FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ati OCA], [https://pdbe.org/1ati PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ati RCSB], [https://www.ebi.ac.uk/pdbsum/1ati PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ati ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ati FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ati OCA], [http://www.ebi.ac.uk/pdbsum/1ati PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ati RCSB]</span>
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[https://www.uniprot.org/uniprot/SYG_THET8 SYG_THET8] Catalyzes the attachment of glycine to tRNA(Gly) (By similarity).[HAMAP-Rule:MF_00253_B]
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}}
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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/at/1ati_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=1ati ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF GLYCYL-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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The sequence and crystal structure at 2.75 A resolution of the homodimeric glycyl-tRNA synthetase from Thermus thermophilus, the first representative of the last unknown class II synthetase subgroup, have been determined. The three class II synthetase sequence motifs are present but the structure was essential for identification of motif 1, which does not possess the proline previously believed to be an essential class II invariant. Nevertheless, crucial contacts with the active site of the other monomer involving motif 1 are conserved and a more comprehensive description of class II now becomes possible. Each monomer consists of an active site strongly resembling that of the aspartyl and seryl enzymes, a C-terminal anticodon recognition domain of 100 residues and a third domain unusually inserted between motifs 1 and 2 almost certainly interacting with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel five-stranded parallel-antiparallel beta-sheet structure with three surrounding helices. The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA synthetase due to the conserved nature of the class II active site.
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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: Kern D]]
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1ATI 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=1ATI OCA].
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[[Category: Logan DT]]
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[[Category: Mazauric M-H]]
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==Reference==
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[[Category: Moras D]]
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Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus., Logan DT, Mazauric MH, Kern D, Moras D, EMBO J. 1995 Sep 1;14(17):4156-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7556056 7556056]
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[[Category: Glycine--tRNA ligase]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
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[[Category: Kern, D.]]
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[[Category: Logan, D T.]]
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[[Category: Mazauric, M H.]]
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[[Category: Moras, D.]]
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[[Category: aminoacyl-trna synthetase]]
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[[Category: ligase]]
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[[Category: protein biosynthesis]]
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[[Category: synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:47:13 2008''
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Current revision

CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

PDB ID 1ati

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