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3qe4

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<StructureSection load='3qe4' size='340' side='right'caption='[[3qe4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3qe4' size='340' side='right'caption='[[3qe4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qe4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QE4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qe4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QE4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CF:4-CYANO-L-PHENYLALANINE'>4CF</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ag6|2ag6]], [[1zh0|1zh0]], [[1zh6|1zh6]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CF:4-CYANO-L-PHENYLALANINE'>4CF</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0389, TyrRS, tyrS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe4 OCA], [https://pdbe.org/3qe4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qe4 RCSB], [https://www.ebi.ac.uk/pdbsum/3qe4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qe4 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=3qe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe4 OCA], [https://pdbe.org/3qe4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qe4 RCSB], [https://www.ebi.ac.uk/pdbsum/3qe4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qe4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SYY_METJA SYY_METJA]] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).<ref>PMID:10585437</ref>
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[https://www.uniprot.org/uniprot/SYY_METJA SYY_METJA] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).<ref>PMID:10585437</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have employed a rapid fluorescence-based screen to assess the polyspecificity of several aminoacyl-tRNA synthetases (aaRSs) against an array of unnatural amino acids. We discovered that a p-cyanophenylalanine specific aminoacyl-tRNA synthetase (pCNF-RS) has high substrate permissivity for unnatural amino acids, while maintaining its ability to discriminate against the 20 canonical amino acids. This orthogonal pCNF-RS, together with its cognate amber nonsense suppressor tRNA, is able to selectively incorporate 18 unnatural amino acids into proteins, including trifluoroketone-, alkynyl-, and halogen-substituted amino acids. In an attempt to improve our understanding of this polyspecificity, the X-ray crystal structure of the aaRS-p-cyanophenylalanine complex was determined. A comparison of this structure with those of other mutant aaRSs showed that both binding site size and other more subtle features control substrate polyspecificity.
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An Evolved Aminoacyl-tRNA Synthetase with Atypical Polysubstrate Specificity .,Young DD, Young TS, Jahnz M, Ahmad I, Spraggon G, Schultz PG Biochemistry. 2011 Feb 1. PMID:21280675<ref>PMID:21280675</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qe4" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43067]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Tyrosine--tRNA ligase]]
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[[Category: Methanocaldococcus jannaschii]]
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[[Category: Ahmad, I]]
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[[Category: Ahmad I]]
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[[Category: Jahnz, M]]
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[[Category: Jahnz M]]
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[[Category: Schultz, P G]]
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[[Category: Schultz PG]]
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[[Category: Spraggon, G]]
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[[Category: Spraggon G]]
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[[Category: Young, D D]]
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[[Category: Young DD]]
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[[Category: Young, T S]]
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[[Category: Young TS]]
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[[Category: Evolved trna synthetase]]
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[[Category: Ligase]]
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[[Category: Trna]]
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[[Category: Trna synthetase evolved to bind unnatural amino acid]]
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Current revision

An evolved aminoacyl-tRNA Synthetase with atypical polysubstrate specificity

PDB ID 3qe4

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