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7ta8

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<StructureSection load='7ta8' size='340' side='right'caption='[[7ta8]]' scene=''>
<StructureSection load='7ta8' size='340' side='right'caption='[[7ta8]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TA8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7ta8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TA8 FirstGlance]. <br>
</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=7ta8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ta8 OCA], [https://pdbe.org/7ta8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ta8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ta8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ta8 ProSAT]</span></td></tr>
</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=7ta8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ta8 OCA], [https://pdbe.org/7ta8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ta8 RCSB], [https://www.ebi.ac.uk/pdbsum/7ta8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ta8 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fluorosubstituted tryptophans serve as valuable probes for fluorescence and nuclear magnetic resonance (NMR) studies of proteins. Here, we describe an unusual photoreactivity introduced by replacing the single tryptophan in cyclophilin A with 7-fluoro-tryptophan. UV exposure at 282 nm defluorinates 7-fluoro-tryptophan and crosslinks it to a nearby phenylalanine, generating a bright fluorophore. The crosslink-containing fluorescent protein possesses a large quantum yield of approximately 0.40 with a fluorescence lifetime of 2.38 ns. The chemical nature of the crosslink and the three-dimensional protein structure were determined by mass spectrometry and NMR spectroscopy. To the best of our knowledge, this is the first report of a Phe-Trp crosslink in a protein. Our finding may break new ground for developing novel fluorescence probes and for devising new strategies to exploit aromatic crosslinks in proteins.
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The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink.,Lu M, Toptygin D, Xiang Y, Shi Y, Schwieters CD, Lipinski EC, Ahn J, Byeon IL, Gronenborn AM J Am Chem Soc. 2022 Jun 22;144(24):10809-10816. doi: 10.1021/jacs.2c02054. Epub, 2022 May 14. PMID:35574633<ref>PMID:35574633</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7ta8" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ahn J]]
[[Category: Ahn J]]

Revision as of 20:38, 12 April 2023

NMR structure of crosslinked cyclophilin A

PDB ID 7ta8

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