4wj4: Difference between revisions

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==structure of protein-tRNA complex==
 
<StructureSection load='4wj4' size='340' side='right' caption='[[4wj4]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
==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]] 3.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4wj4]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WJ4 FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.294&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wj3|4wj3]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate--tRNA(Asn)_ligase Aspartate--tRNA(Asn) ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.23 6.1.1.23] </span></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>
<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=4wj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wj4 RCSB], [http://www.ebi.ac.uk/pdbsum/4wj4 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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)]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Kato, K]]
[[Category: Large Structures]]
[[Category: Nakamura, A]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Suzuki, T]]
[[Category: Kato K]]
[[Category: Tanaka, I]]
[[Category: Nakamura A]]
[[Category: Yao, M]]
[[Category: Suzuki T]]
[[Category: Aminoacylation]]
[[Category: Tanaka I]]
[[Category: Ligase-rna complex]]
[[Category: Yao M]]
[[Category: Non-discriminating aspr]]
[[Category: Trna]]

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

4wj4 is a 2 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.294Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1]

See Also

References

  1. ↑ Bernard D, Akochy PM, Beaulieu D, Lapointe J, Roy PH. Two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase from Pseudomonas aeruginosa are individually implicated in the recognition of tRNAAsn. J Bacteriol. 2006 Jan;188(1):269-74. PMID:16352843 doi:http://dx.doi.org/10.1128/JB.188.1.269-274.2006

4wj4, resolution 3.29Å

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