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| | <StructureSection load='5k1p' size='340' side='right'caption='[[5k1p]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='5k1p' size='340' side='right'caption='[[5k1p]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k1p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43340_[[methanococcus_frisius_blotevogel_et_al._1986]] Atcc 43340 [[methanococcus frisius blotevogel et al. 1986]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K1P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k1p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K1P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.499Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k1x|5k1x]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pylS, MM_1445 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2209 ATCC 43340 [[Methanococcus frisius Blotevogel et al. 1986]]])</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=5k1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1p OCA], [https://pdbe.org/5k1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k1p RCSB], [https://www.ebi.ac.uk/pdbsum/5k1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1p 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/Pyrrolysine--tRNA(Pyl)_ligase Pyrrolysine--tRNA(Pyl) ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.26 6.1.1.26] </span></td></tr>
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| - | <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=5k1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1p OCA], [http://pdbe.org/5k1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k1p RCSB], [http://www.ebi.ac.uk/pdbsum/5k1p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYLS_METMA PYLS_METMA]] Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG (By similarity). | + | [https://www.uniprot.org/uniprot/PYLS_METMA PYLS_METMA] Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Weber, A]] | + | [[Category: Methanosarcina mazei]] |
| - | [[Category: Aminoacyl-trna synthetase]] | + | [[Category: Weber A]] |
| - | [[Category: Ligase]]
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| - | [[Category: Noncanonical amino acid]]
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| - | [[Category: Protein engineering]]
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| Structural highlights
Function
PYLS_METMA Catalyzes the attachment of pyrrolysine to tRNA(Pyl). Pyrrolysine is a lysine derivative encoded by the termination codon UAG (By similarity).
Publication Abstract from PubMed
Fluorophenylalanines bearing 2-5 fluorine atoms at the phenyl ring have been genetically encoded by amber codon. Replacement of F59, a phenylalanine residue that is directly involved in interactions with trimethylated K9 of histone H3, in the Mpp8 chromodomain recombinantly with fluorophenylalanines significantly impairs the binding to a K9-trimethylated H3 peptide.
Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader.,Lee YJ, Schmidt MJ, Tharp JM, Weber A, Koenig AL, Zheng H, Gao J, Waters ML, Summerer D, Liu WR Chem Commun (Camb). 2016 Oct 18;52(85):12606-12609. PMID:27711380[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lee YJ, Schmidt MJ, Tharp JM, Weber A, Koenig AL, Zheng H, Gao J, Waters ML, Summerer D, Liu WR. Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader. Chem Commun (Camb). 2016 Oct 18;52(85):12606-12609. PMID:27711380 doi:http://dx.doi.org/10.1039/c6cc05959g
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