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[[ | ==Ternary complex of E. coli leucyl-tRNA synthetase, tRNA(leu) and the benzoxaborole AN2679 in the editing conformation== | ||
<StructureSection load='4ari' size='340' side='right' caption='[[4ari]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ari]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ARI FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=N79:[(1S,5R,6R,8R)-6-(6-AMINOPURIN-9-YL)SPIRO[2,4,7-TRIOXA-3-BORANUIDABICYCLO[3.3.0]OCTANE-3,9-8-OXA-9-BORANUIDABICYCLO[4.3.0]NONA-1(6),2,4-TRIENE]-8-YL]METHYL+DIHYDROGEN+PHOSPHATE'>N79</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ajg|2ajg]], [[2ajh|2ajh]], [[2aji|2aji]], [[4aq7|4aq7]], [[4arc|4arc]], [[4as1|4as1]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucine--tRNA_ligase Leucine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.4 6.1.1.4] </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=4ari FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ari OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ari RCSB], [http://www.ebi.ac.uk/pdbsum/4ari PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Leucyl-tRNA synthetase (LeuRS) produces error-free leucyl-tRNA(Leu) by coordinating translocation of the 3' end of (mis-)charged tRNAs from its synthetic site to a separate proofreading site for editing. Here we report cocrystal structures of the Escherichia coli LeuRS-tRNA(Leu) complex in the aminoacylation or editing conformations, showing that translocation involves correlated rotations of four flexibly linked LeuRS domains. This pivots the tRNA to guide its charged 3' end from the closed aminoacylation state to the editing site. The editing domain unexpectedly stabilizes the tRNA during aminoacylation, and a large rotation of the leucine-specific domain positions the conserved KMSKS loop to bind the 3' end of the tRNA, promoting catalysis. Our results give new insight into the structural dynamics of a molecular machine that is essential for accurate protein synthesis. | |||
Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase.,Palencia A, Crepin T, Vu MT, Lincecum TL Jr, Martinis SA, Cusack S Nat Struct Mol Biol. 2012 Jun 10. doi: 10.1038/nsmb.2317. PMID:22683997<ref>PMID:22683997</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Leucine--tRNA ligase]] | [[Category: Leucine--tRNA ligase]] | ||
[[Category: Crepin, T | [[Category: Crepin, T]] | ||
[[Category: Cusack, S | [[Category: Cusack, S]] | ||
[[Category: Jr, T L.Lincecum | [[Category: Jr, T L.Lincecum]] | ||
[[Category: Martinis, S A | [[Category: Martinis, S A]] | ||
[[Category: Palencia, A | [[Category: Palencia, A]] | ||
[[Category: Vu, M T | [[Category: Vu, M T]] | ||
[[Category: Class i aminoacyl-trna synthetase]] | [[Category: Class i aminoacyl-trna synthetase]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
[[Category: Ligase-rna complex]] | [[Category: Ligase-rna complex]] | ||
[[Category: Protein biosynthesis]] | [[Category: Protein biosynthesis]] | ||
Revision as of 17:08, 4 January 2015
Ternary complex of E. coli leucyl-tRNA synthetase, tRNA(leu) and the benzoxaborole AN2679 in the editing conformationTernary complex of E. coli leucyl-tRNA synthetase, tRNA(leu) and the benzoxaborole AN2679 in the editing conformation
Structural highlights
Publication Abstract from PubMedLeucyl-tRNA synthetase (LeuRS) produces error-free leucyl-tRNA(Leu) by coordinating translocation of the 3' end of (mis-)charged tRNAs from its synthetic site to a separate proofreading site for editing. Here we report cocrystal structures of the Escherichia coli LeuRS-tRNA(Leu) complex in the aminoacylation or editing conformations, showing that translocation involves correlated rotations of four flexibly linked LeuRS domains. This pivots the tRNA to guide its charged 3' end from the closed aminoacylation state to the editing site. The editing domain unexpectedly stabilizes the tRNA during aminoacylation, and a large rotation of the leucine-specific domain positions the conserved KMSKS loop to bind the 3' end of the tRNA, promoting catalysis. Our results give new insight into the structural dynamics of a molecular machine that is essential for accurate protein synthesis. Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase.,Palencia A, Crepin T, Vu MT, Lincecum TL Jr, Martinis SA, Cusack S Nat Struct Mol Biol. 2012 Jun 10. doi: 10.1038/nsmb.2317. PMID:22683997[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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