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==Crystal structure of non-discriminating aspartyl-tRNA synthetase from Pseudomonas aeruginosa complexed with tRNA(Asn) and aspartic acid== | |||
<StructureSection load='4wj4' size='340' side='right'caption='[[4wj4]], [[Resolution|resolution]] 3.29Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wj4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WJ4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.294Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wj4 OCA], [https://pdbe.org/4wj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wj4 RCSB], [https://www.ebi.ac.uk/pdbsum/4wj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wj4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SYDND_PSEAE SYDND_PSEAE] Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over tRNA(Asn). 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:16352843</ref> | |||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]] | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Suzuki | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa PAO1]] | ||
[[Category: Kato K]] | |||
[[Category: Nakamura A]] | |||
[[Category: Suzuki T]] | |||
[[Category: Tanaka I]] | |||
[[Category: Yao M]] | |||
Latest revision as of 12:01, 20 March 2024
Crystal structure of non-discriminating aspartyl-tRNA synthetase from Pseudomonas aeruginosa complexed with tRNA(Asn) and aspartic acidCrystal structure of non-discriminating aspartyl-tRNA synthetase from Pseudomonas aeruginosa complexed with tRNA(Asn) and aspartic acid
Structural highlights
FunctionSYDND_PSEAE Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over tRNA(Asn). 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).[1] See AlsoReferences
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