7qut
From Proteopedia
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(New page: '''Unreleased structure''' The entry 7qut is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==serial synchrotron crystallographic structure of Drosophila Melanogaster (6-4) photolyase== | |
| + | <StructureSection load='7qut' size='340' side='right'caption='[[7qut]], [[Resolution|resolution]] 2.24Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7qut]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QUT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.24Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7qut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qut OCA], [https://pdbe.org/7qut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qut RCSB], [https://www.ebi.ac.uk/pdbsum/7qut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qut ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q0E8P0_DROME Q0E8P0_DROME] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We present the structure of a photoactivated animal (6-4) photolyase in its radical pair state, captured by serial crystallography. We observe how a conserved asparigine moves towards the semiquinone FAD chromophore and stabilizes it by hydrogen bonding. Several amino acids around the final tryptophan radical rearrange, opening it up to the solvent. The structure explains how the protein environment stabilizes the radical pair state, which is crucial for function of (6-4) photolyases and cryptochromes. | ||
| - | + | Structural basis of the radical pair state in photolyases and cryptochromes.,Cellini A, Shankar MK, Wahlgren WY, Nimmrich A, Furrer A, James D, Wranik M, Aumonier S, Beale EV, Dworkowski F, Standfuss J, Weinert T, Westenhoff S Chem Commun (Camb). 2022 Mar 30. doi: 10.1039/d2cc00376g. PMID:35352724<ref>PMID:35352724</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7qut" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cellini A]] | ||
| + | [[Category: Kumar MS]] | ||
| + | [[Category: Weixiao YW]] | ||
| + | [[Category: Westenhoff S]] | ||
Current revision
serial synchrotron crystallographic structure of Drosophila Melanogaster (6-4) photolyase
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