1n9w

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[[Image:1n9w.jpg|left|200px]]
 
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==Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase from Thermus thermophilus==
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The line below this paragraph, containing "STRUCTURE_1n9w", creates the "Structure Box" on the page.
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<StructureSection load='1n9w' size='340' side='right'caption='[[1n9w]], [[Resolution|resolution]] 2.30&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'>[[1n9w]] is a 2 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=1N9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N9W 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]] 2.3&#8491;</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=1n9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9w OCA], [https://pdbe.org/1n9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n9w RCSB], [https://www.ebi.ac.uk/pdbsum/1n9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9w ProSAT]</span></td></tr>
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{{STRUCTURE_1n9w| PDB=1n9w | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYDND_THET8 SYDND_THET8] Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn) with similar efficiencies. Reaction proceeds in two steps: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).<ref>PMID:10727213</ref> <ref>PMID:9220965</ref>
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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/n9/1n9w_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=1n9w ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the non-discriminating and archaeal-type aspartyl-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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== References ==
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==Overview==
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<references/>
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In most organisms, tRNA aminoacylation is ensured by 20 aminoacyl-tRNA synthetases (aaRSs). In eubacteria, however, synthetases can be duplicated as in Thermus thermophilus, which contains two distinct AspRSs. While AspRS-1 is specific, AspRS-2 is non-discriminating and aspartylates tRNA(Asp) and tRNA(Asn). The structure at 2.3 A resolution of AspRS-2, the first of a non-discriminating synthetase, was solved. It differs from that of AspRS-1 but has resemblance to that of discriminating and archaeal AspRS from Pyrococcus kodakaraensis. The protein presents non-conventional features in its OB-fold anticodon-binding domain, namely the absence of a helix inserted between two beta-strands of this fold and a peculiar L1 loop differing from the large loops known to interact with tRNA(Asp) identity determinant C36 in conventional AspRSs. In AspRS-2, this loop is small and structurally homologous to that in AsnRSs, including conservation of a proline. In discriminating Pyrococcus AspRS, the L1 loop, although small, lacks this proline and is not superimposable with that of AspRS-2 or AsnRS. Its particular status is demonstrated by a loop-exchange experiment that renders the Pyrococcus AspRS non-discriminating.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1N9W 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=1N9W OCA].
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==Reference==
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Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain., Charron C, Roy H, Blaise M, Giege R, Kern D, EMBO J. 2003 Apr 1;22(7):1632-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12660169 12660169]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Blaise, M.]]
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[[Category: Blaise M]]
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[[Category: Charron, C.]]
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[[Category: Charron C]]
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[[Category: Giege, R.]]
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[[Category: Giege R]]
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[[Category: Kern, D.]]
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[[Category: Kern D]]
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[[Category: Roy, H.]]
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[[Category: Roy H]]
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[[Category: Biosynthetic protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:16:30 2008''
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Current revision

Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase from Thermus thermophilus

PDB ID 1n9w

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