3prh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='3prh' size='340' side='right'caption='[[3prh]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3prh' size='340' side='right'caption='[[3prh]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3prh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3prh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PRH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=3prh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3prh OCA], [https://pdbe.org/3prh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3prh RCSB], [https://www.ebi.ac.uk/pdbsum/3prh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3prh ProSAT]</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=3prh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3prh OCA], [https://pdbe.org/3prh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3prh RCSB], [https://www.ebi.ac.uk/pdbsum/3prh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3prh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SYW_BACSU SYW_BACSU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 25: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Antonczak AK]] | |||
[[Category: Antonczak | [[Category: Bochtler M]] | ||
[[Category: Bochtler | [[Category: Brancale A]] | ||
[[Category: Brancale | [[Category: Czapinska H]] | ||
[[Category: Czapinska | [[Category: Piasecka A]] | ||
[[Category: Piasecka | [[Category: Simova Z]] | ||
[[Category: Simova | [[Category: Tippmann EM]] | ||
[[Category: Tippmann | [[Category: Yonemoto I]] | ||
[[Category: Yonemoto | |||
Latest revision as of 12:59, 6 September 2023
tryptophanyl-tRNA synthetase Val144Pro mutant from B. subtilistryptophanyl-tRNA synthetase Val144Pro mutant from B. subtilis
Structural highlights
FunctionPublication Abstract from PubMedThe site-selective encoding of noncanonical amino acids (NAAs) is a powerful technique for the installation of novel chemical functional groups in proteins. This is often achieved by recoding a stop codon and requires two additional components: an evolved aminoacyl tRNA synthetase (AARS) and a cognate tRNA. Analysis of the most successful AARSs reveals common characteristics. The highest fidelity NAA systems derived from the Methanocaldococcus jannaschii tyrosyl AARS feature specific mutations to two residues reported to interact with the hydroxyl group of the substrate tyrosine. We demonstrate that the restoration of just one of these determinants for amino acid specificity results in the loss of fidelity as the evolved AARSs become noticeably promiscuous. These results offer a partial explanation of a recently retracted strategy for the synthesis of glycoproteins. Similarly, we reinvestigated a tryptophanyl AARS reported to allow the site-selective incorporation of 5-hydroxy tryptophan within mammalian cells. In multiple experiments, the enzyme displayed elements of promiscuity despite its previous characterization as a high fidelity enzyme. Given the many similarities of the TyrRSs and TrpRSs reevaluated here, our findings can be largely combined, and in doing so they reinforce the long-established central dogma regarding the molecular basis by which these enzymes contribute to the fidelity of translation. Thus, our view is that the central claims of fidelity reported in several NAA systems remain unproven and unprecedented. Importance of single molecular determinants in the fidelity of expanded genetic codes.,Antonczak AK, Simova Z, Yonemoto IT, Bochtler M, Piasecka A, Czapinska H, Brancale A, Tippmann EM Proc Natl Acad Sci U S A. 2011 Jan 11. PMID:21224416[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||