1n9w

<StructureSection load='1n9w' size='340' side='right' caption='[[1n9w]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[1n9w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N9W FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9w OCA], [http://pdbe.org/1n9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n9w RCSB], [http://www.ebi.ac.uk/pdbsum/1n9w PDBsum]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n9/1n9w_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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:12660169<ref>PMID:12660169</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1n9w" style="background-color:#fffaf0;"></div>

*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Blaise, M]]

[[Category: Charron, C]]

[[Category: Giege, R]]

[[Category: Kern, D]]

[[Category: Roy, H]]

[[Category: Biosynthetic protein]]