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| ==Crystal structure of tyrosyl-tRNA synthetase complexed with p-(2-tetrazolyl)-phenylalanine== | | ==Crystal structure of tyrosyl-tRNA synthetase complexed with p-(2-tetrazolyl)-phenylalanine== |
- | <StructureSection load='3n2y' size='340' side='right' caption='[[3n2y]], [[Resolution|resolution]] 2.49Å' scene=''> | + | <StructureSection load='3n2y' size='340' side='right'caption='[[3n2y]], [[Resolution|resolution]] 2.49Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3n2y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N2Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N2Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3n2y]] 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=3N2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N2Y FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TEF:4-(2H-TETRAZOL-2-YL)-L-PHENYLALANINE'>TEF</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tyrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TEF:4-(2H-TETRAZOL-2-YL)-L-PHENYLALANINE'>TEF</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] </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=3n2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2y OCA], [https://pdbe.org/3n2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n2y RCSB], [https://www.ebi.ac.uk/pdbsum/3n2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2y 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=3n2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2y OCA], [http://pdbe.org/3n2y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n2y RCSB], [http://www.ebi.ac.uk/pdbsum/3n2y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2y ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://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> | + | [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> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
- | *[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]] | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Atcc 43067]] | + | [[Category: Large Structures]] |
- | [[Category: Tyrosine--tRNA ligase]] | + | [[Category: Methanocaldococcus jannaschii]] |
- | [[Category: Li, J]] | + | [[Category: Li J]] |
- | [[Category: Wu, M]] | + | [[Category: Wu M]] |
- | [[Category: Zang, J]] | + | [[Category: Zang J]] |
- | [[Category: Aminoacyl-trna synthetase]]
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- | [[Category: Ligase]]
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- | [[Category: Photoclick chemistry]]
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| Structural highlights
Function
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).[1]
Publication Abstract from PubMed
Light-induced chemical reactions exist in nature, regulating many important cellular and organismal functions, e.g., photosensing in prokaryotes and vision formation in mammals. Here, we report the genetic incorporation of a photoreactive unnatural amino acid, p-(2-tetrazole)phenylalanine (p-Tpa), into myoglobin site-specifically in E. coli by evolving an orthogonal tRNA/aminoacyl-tRNA synthetase pair and the use of p-Tpa as a bioorthogonal chemical "handle" for fluorescent labeling of p-Tpa-encoded myoglobin via the photoclick reaction. Moreover, we elucidated the structural basis for the biosynthetic incorporation of p-Tpa into proteins by solving the X-ray structure of p-Tpa-specific aminoacyl-tRNA synthetase in complex with p-Tpa. The genetic encoding of this photoreactive amino acid should make it possible in the future to photoregulate protein function in living systems.
A biosynthetic route to photoclick chemistry on proteins.,Wang J, Zhang W, Song W, Wang Y, Yu Z, Li J, Wu M, Wang L, Zang J, Lin Q J Am Chem Soc. 2010 Oct 27;132(42):14812-8. PMID:20919707[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Steer BA, Schimmel P. Major anticodon-binding region missing from an archaebacterial tRNA synthetase. J Biol Chem. 1999 Dec 10;274(50):35601-6. PMID:10585437
- ↑ Wang J, Zhang W, Song W, Wang Y, Yu Z, Li J, Wu M, Wang L, Zang J, Lin Q. A biosynthetic route to photoclick chemistry on proteins. J Am Chem Soc. 2010 Oct 27;132(42):14812-8. PMID:20919707 doi:10.1021/ja104350y
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