4cs2: Difference between revisions
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==Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in its apo form== | ==Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in its apo form== | ||
<StructureSection load='4cs2' size='340' side='right' caption='[[4cs2]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4cs2' size='340' side='right' caption='[[4cs2]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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> | <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> | ||
<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=4cs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cs2 RCSB], [http://www.ebi.ac.uk/pdbsum/4cs2 PDBsum]</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=4cs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs2 OCA], [http://pdbe.org/4cs2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cs2 RCSB], [http://www.ebi.ac.uk/pdbsum/4cs2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cs2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4cs2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 15:30, 4 August 2016
Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in its apo formCatalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in its apo form
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 PubMedThe site-selective introduction of photo-crosslinking groups into proteins enables the discovery and mapping of weak and/or transient protein interactions with high spatiotemporal resolution, both in vitro and in vivo. We report the genetic encoding of a furan-based, photo-crosslinking amino acid in human cells; it can be activated with red light, thus offering high penetration depths in biological samples. This is achieved by activation of the amino acid and charging to its cognate tRNA by a pyrrolysyl-tRNA-synthetase (PylRS) mutant with broad polyspecificity. To gain insights into the recognition of this amino acid and to provide a rationale for its polyspecificity, we solved three crystal structures of the PylRS mutant: in its apo-form, in complex with adenosine 5'-(beta,gamma-imido)triphosphate (AMP-PNP) and in complex with the AMP ester of the furan amino acid. These structures provide clues for the observed polyspecificity and represent a promising starting point for the engineering of PylRS mutants with further increased substrate scope. Structural Basis of Furan-Amino Acid Recognition by a Polyspecific Aminoacyl-tRNA-Synthetase and its Genetic Encoding in Human Cells.,Schmidt MJ, Weber A, Pott M, Welte W, Summerer D Chembiochem. 2014 Apr 15. doi: 10.1002/cbic.201402006. PMID:24737732[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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