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1n9w
From Proteopedia
(Difference between revisions)
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<StructureSection load='1n9w' size='340' side='right' caption='[[1n9w]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1n9w' size='340' side='right' caption='[[1n9w]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1n9w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <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://www.rcsb.org/pdb/explore.do?structureId=1n9w RCSB], [http://www.ebi.ac.uk/pdbsum/1n9w PDBsum]</span></td></tr> | + | </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> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1n9w" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] |
[[Category: Blaise, M]] | [[Category: Blaise, M]] | ||
[[Category: Charron, C]] | [[Category: Charron, C]] | ||
Revision as of 23:13, 9 September 2015
Crystal structure of the non-discriminating and archaeal-type aspartyl-tRNA synthetase from Thermus thermophilus
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