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4wj3

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Revision as of 18:36, 11 August 2016

Warning: this is a large structure, and loading might take a long time or not happen at all.

Crystal structure of the asparagine transamidosome from Pseudomonas aeruginosa

Structural highlights

4wj3 is a 20 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	4wj4
Activity:	Glutaminyl-tRNA synthase (glutamine-hydrolyzing), with EC number 6.3.5.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Warning: this is a large structure, and loading might take a long time or not happen at all.

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] [GATA_PSEAE] Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). [GATC_PSEAE] Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). [GATB_PSEAE] Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).

Publication Abstract from PubMed

Many prokaryotes lack a tRNA synthetase to attach asparagine to its cognate tRNAAsn, and instead synthesize asparagine from tRNAAsn-bound aspartate. This conversion involves two enzymes: a nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) that forms Asp-tRNAAsn, and a heterotrimeric amidotransferase GatCAB that amidates Asp-tRNAAsn to form Asn-tRNAAsn for use in protein synthesis. ND-AspRS, GatCAB, and tRNAAsn may assemble in an approximately 400-kDa complex, known as the Asn-transamidosome, which couples the two steps of asparagine biosynthesis in space and time to yield Asn-tRNAAsn. We report the 3.7-A resolution crystal structure of the Pseudomonas aeruginosa Asn-transamidosome, which represents the most common machinery for asparagine biosynthesis in bacteria. We show that, in contrast to a previously described archaeal-type transamidosome, a bacteria-specific GAD domain of ND-AspRS provokes a principally new architecture of the complex. Both tRNAAsn molecules in the transamidosome simultaneously serve as substrates and scaffolds for the complex assembly. This architecture rationalizes an elevated dynamic and a greater turnover of ND-AspRS within bacterial-type transamidosomes, and possibly may explain a different evolutionary pathway of GatCAB in organisms with bacterial-type vs. archaeal-type Asn-transamidosomes. Importantly, because the two-step pathway for Asn-tRNAAsn formation evolutionarily preceded the direct attachment of Asn to tRNAAsn, our structure also may reflect the mechanism by which asparagine was initially added to the genetic code.

Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis.,Suzuki T, Nakamura A, Kato K, Soll D, Tanaka I, Sheppard K, Yao M Proc Natl Acad Sci U S A. 2014 Dec 29. pii: 201423314. PMID:25548166^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Suzuki T, Nakamura A, Kato K, Soll D, Tanaka I, Sheppard K, Yao M. Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis. Proc Natl Acad Sci U S A. 2014 Dec 29. pii: 201423314. PMID:25548166 doi:http://dx.doi.org/10.1073/pnas.1423314112

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wj3"

@@ Line 1: / Line 1: @@
+{{Large structure}}
 ==Crystal structure of the asparagine transamidosome from Pseudomonas aeruginosa==
 <StructureSection load='4wj3' size='340' side='right' caption='[[4wj3]], [[Resolution|resolution]] 3.71&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wj4|4wj4]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-tRNA_synthase_(glutamine-hydrolyzing) Glutaminyl-tRNA synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.7 6.3.5.7] </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=4wj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wj3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wj3 PDBsum]</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=4wj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wj3 OCA], [http://pdbe.org/4wj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wj3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wj3 ProSAT]</span></td></tr>
 </table>
+{{Large structure}}
 == 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>  [[http://www.uniprot.org/uniprot/GATA_PSEAE GATA_PSEAE]] Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). [[http://www.uniprot.org/uniprot/GATC_PSEAE GATC_PSEAE]] Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). [[http://www.uniprot.org/uniprot/GATB_PSEAE GATB_PSEAE]] Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
@@ Line 18: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4wj3" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[TRNA|TRNA]]
 == References ==
 <references/>

4wj3

From Proteopedia

Revision as of 18:36, 11 August 2016

Crystal structure of the asparagine transamidosome from Pseudomonas aeruginosa

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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