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==Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in complex with AMPPNP== | ==Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in complex with AMPPNP== | ||
<StructureSection load='4cs4' size='340' side='right' caption='[[4cs4]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='4cs4' size='340' side='right'caption='[[4cs4]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
[[4cs4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CS4 OCA]. <br> | <table><tr><td colspan='2'>[[4cs4]] 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=4CS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CS4 FirstGlance]. <br> | ||
<b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=AXZ:2-{[DIHYDROXY(4-AMINOETHYLPHENYL)-{4}-SULFANYL]AMINO}-3-HYDROXYPROPANOIC+ACID'>AXZ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>< | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.349Å</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=AXZ:2-{[DIHYDROXY(4-AMINOETHYLPHENYL)-{4}-SULFANYL]AMINO}-3-HYDROXYPROPANOIC+ACID'>AXZ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4cs4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs4 OCA], [https://pdbe.org/4cs4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cs4 RCSB], [https://www.ebi.ac.uk/pdbsum/4cs4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cs4 ProSAT]</span></td></tr> | ||
<b>Resources:</b> <span class='plainlinks'>[ | </table> | ||
== 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;"> | |||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The 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. | The 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. | ||
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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<ref>PMID:24737732</ref> | 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<ref>PMID:24737732</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 4cs4" 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: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Methanosarcina mazei]] | ||
[[Category: | [[Category: Pott M]] | ||
[[Category: | [[Category: Schmidt MJ]] | ||
[[Category: | [[Category: Summerer D]] | ||
[[Category: | [[Category: Weber A]] | ||
[[Category: | [[Category: Welte W]] | ||
Latest revision as of 14:13, 9 May 2024
Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in complex with AMPPNPCatalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in complex with AMPPNP
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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