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| | ==Crystal Structure Of A Mutant M. Jannashii Tyrosyl-tRNA Synthetase== | | ==Crystal Structure Of A Mutant M. Jannashii Tyrosyl-tRNA Synthetase== |
| - | <StructureSection load='5u36' size='340' side='right' caption='[[5u36]], [[Resolution|resolution]] 3.03Å' scene=''> | + | <StructureSection load='5u36' size='340' side='right'caption='[[5u36]], [[Resolution|resolution]] 3.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5u36]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U36 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U36 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5u36]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U36 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j1u|1j1u]], [[1u7d|1u7d]]</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]] 3.03Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tyrS, MJ0389 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</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=5u36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u36 OCA], [https://pdbe.org/5u36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u36 RCSB], [https://www.ebi.ac.uk/pdbsum/5u36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u36 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5u36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u36 OCA], [http://pdbe.org/5u36 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u36 RCSB], [http://www.ebi.ac.uk/pdbsum/5u36 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u36 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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| | </div> | | </div> |
| | <div class="pdbe-citations 5u36" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5u36" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Metja]] | + | [[Category: Large Structures]] |
| - | [[Category: Tyrosine--tRNA ligase]] | + | [[Category: Methanocaldococcus jannaschii DSM 2661]] |
| - | [[Category: Fu, G]] | + | [[Category: Fu G]] |
| - | [[Category: Luo, X]] | + | [[Category: Luo X]] |
| - | [[Category: Wang, F]] | + | [[Category: Wang F]] |
| - | [[Category: Wilson, I A]] | + | [[Category: Wilson IA]] |
| - | [[Category: Zhu, X]] | + | [[Category: Zhu X]] |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Tyrosine phosphorylation]]
| + | |
| 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
Tyrosine phosphorylation is a common protein post-translational modification that plays a critical role in signal transduction and the regulation of many cellular processes. Using a propeptide strategy to increase cellular uptake of O-phosphotyrosine (pTyr) and its nonhydrolyzable analog 4-phosphomethyl-L-phenylalanine (Pmp), we identified an orthogonal aminoacyl-tRNA synthetase-tRNA pair that allows site-specific incorporation of both pTyr and Pmp into recombinant proteins in response to the amber stop codon in Escherichia coli in good yields. The X-ray structure of the synthetase reveals a reconfigured substrate-binding site, formed by nonconservative mutations and substantial local structural perturbations. We demonstrate the utility of this method by introducing Pmp into a putative phosphorylation site and determining the affinities of the individual variants for the substrate 3BP2. In summary, this work provides a useful recombinant tool to dissect the biological functions of tyrosine phosphorylation at specific sites in the proteome.
Genetically encoding phosphotyrosine and its nonhydrolyzable analog in bacteria.,Luo X, Fu G, Wang RE, Zhu X, Zambaldo C, Liu R, Liu T, Lyu X, Du J, Xuan W, Yao A, Reed SA, Kang M, Zhang Y, Guo H, Huang C, Yang PY, Wilson IA, Schultz PG, Wang F Nat Chem Biol. 2017 Jun 12. doi: 10.1038/nchembio.2405. PMID:28604693[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
- ↑ Luo X, Fu G, Wang RE, Zhu X, Zambaldo C, Liu R, Liu T, Lyu X, Du J, Xuan W, Yao A, Reed SA, Kang M, Zhang Y, Guo H, Huang C, Yang PY, Wilson IA, Schultz PG, Wang F. Genetically encoding phosphotyrosine and its nonhydrolyzable analog in bacteria. Nat Chem Biol. 2017 Jun 12. doi: 10.1038/nchembio.2405. PMID:28604693 doi:http://dx.doi.org/10.1038/nchembio.2405
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