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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cs2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4cs2]] 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=4CS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CS2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs2 OCA], [https://pdbe.org/4cs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cs2 RCSB], [https://www.ebi.ac.uk/pdbsum/4cs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cs2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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 == | ||
| Line 21: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Aminoacyl tRNA | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Pott | [[Category: Methanosarcina mazei]] | ||
[[Category: Schmidt | [[Category: Pott M]] | ||
[[Category: Summerer | [[Category: Schmidt MJ]] | ||
[[Category: Weber | [[Category: Summerer D]] | ||
[[Category: Welte | [[Category: Weber A]] | ||
[[Category: Welte W]] | |||
Latest revision as of 15:15, 20 December 2023
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
FunctionPYLS_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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