4rr9: Difference between revisions
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<StructureSection load='4rr9' size='340' side='right' caption='[[4rr9]], [[Resolution|resolution]] 1.67Å' scene=''> | <StructureSection load='4rr9' size='340' side='right' caption='[[4rr9]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rr9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RR9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RR9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rr9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpe Aerpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RR9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RR9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3S:SERINE-3-AMINOADENOSINE'>A3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3S:SERINE-3-AMINOADENOSINE'>A3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rr6|4rr6]], [[4rr7|4rr7]], [[4rr8|4rr8]], [[4rra|4rra]], [[4rrb|4rrb]], [[4rrc|4rrc]], [[4rrd|4rrd]], [[4rrf|4rrf]], [[4rrg|4rrg]], [[4rrh|4rrh]], [[4rri|4rri]], [[4rrj|4rrj]], [[4rrk|4rrk]], [[4rrl|4rrl]], [[4rrm|4rrm]], [[4rrq|4rrq]], [[4rrr|4rrr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rr6|4rr6]], [[4rr7|4rr7]], [[4rr8|4rr8]], [[4rra|4rra]], [[4rrb|4rrb]], [[4rrc|4rrc]], [[4rrd|4rrd]], [[4rrf|4rrf]], [[4rrg|4rrg]], [[4rrh|4rrh]], [[4rri|4rri]], [[4rrj|4rrj]], [[4rrk|4rrk]], [[4rrl|4rrl]], [[4rrm|4rrm]], [[4rrq|4rrq]], [[4rrr|4rrr]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thrS2, APE_0117.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 AERPE])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </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=4rr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr9 OCA], [http://pdbe.org/4rr9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rr9 RCSB], [http://www.ebi.ac.uk/pdbsum/4rr9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rr9 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=4rr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rr9 OCA], [http://pdbe.org/4rr9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rr9 RCSB], [http://www.ebi.ac.uk/pdbsum/4rr9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rr9 ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aerpe]] | |||
[[Category: Threonine--tRNA ligase]] | [[Category: Threonine--tRNA ligase]] | ||
[[Category: Ahmad, S]] | [[Category: Ahmad, S]] | ||
Revision as of 12:08, 22 November 2017
N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Ser3AA (snapshot 4)N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Ser3AA (snapshot 4)
Structural highlights
Publication Abstract from PubMedProofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. Here, we show that a unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes. We show, using three distinct archaea, that a side-chain-stripped recognition site is fully capable of solving a subtle discrimination problem. While biochemical probing establishes that RNA plays the catalytic role, mechanistic insights from multiple high-resolution snapshots reveal that differential remodelling of the catalytic core at the RNA-peptide interface provides the determinants for correct proofreading activity. The functional crosstalk between RNA and protein elucidated here suggests how primordial enzyme functions could have emerged on RNA-peptide scaffolds before recruitment of specific side chains. Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.,Ahmad S, Muthukumar S, Kuncha SK, Routh SB, Yerabham AS, Hussain T, Kamarthapu V, Kruparani SP, Sankaranarayanan R Nat Commun. 2015 Jun 26;6:7552. doi: 10.1038/ncomms8552. PMID:26113036[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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