6yrx
From Proteopedia
(Difference between revisions)
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==Low-dose crystal structure of FAP at room temperature== | ==Low-dose crystal structure of FAP at room temperature== | ||
| - | <StructureSection load='6yrx' size='340' side='right'caption='[[6yrx]]' scene=''> | + | <StructureSection load='6yrx' size='340' side='right'caption='[[6yrx]], [[Resolution|resolution]] 1.87Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YRX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6yrx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorella_variabilis Chlorella variabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YRX 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=6yrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yrx OCA], [https://pdbe.org/6yrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yrx RCSB], [https://www.ebi.ac.uk/pdbsum/6yrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yrx ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87Å</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=STE:STEARIC+ACID'>STE</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=6yrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yrx OCA], [https://pdbe.org/6yrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yrx RCSB], [https://www.ebi.ac.uk/pdbsum/6yrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yrx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FAP_CHLVA FAP_CHLVA] Catalyzes the decarboxylation of free fatty acids to n-alkanes or n-alkenes in response to blue light (PubMed:28860382, PubMed:30106504, PubMed:30673222). Substrate preference is toward fatty acids with C16 or C17 chains (PubMed:28860382, PubMed:30106504, PubMed:30673222). Saturated fatty acids are converted to alkanes, not alkenes (PubMed:28860382). The decarboxylation is initiated through electron abstraction from the fatty acid by the photo-excited FAD (PubMed:28860382).<ref>PMID:28860382</ref> <ref>PMID:30106504</ref> <ref>PMID:30673222</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fatty acid photodecarboxylase (FAP) is a photoenzyme with potential green chemistry applications. By combining static, time-resolved, and cryotrapping spectroscopy and crystallography as well as computation, we characterized Chlorella variabilis FAP reaction intermediates on time scales from subpicoseconds to milliseconds. High-resolution crystal structures from synchrotron and free electron laser x-ray sources highlighted an unusual bent shape of the oxidized flavin chromophore. We demonstrate that decarboxylation occurs directly upon reduction of the excited flavin by the fatty acid substrate. Along with flavin reoxidation by the alkyl radical intermediate, a major fraction of the cleaved carbon dioxide unexpectedly transformed in 100 nanoseconds, most likely into bicarbonate. This reaction is orders of magnitude faster than in solution. Two strictly conserved residues, R451 and C432, are essential for substrate stabilization and functional charge transfer. | ||
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| + | Mechanism and dynamics of fatty acid photodecarboxylase.,Sorigue D, Hadjidemetriou K, Blangy S, Gotthard G, Bonvalet A, Coquelle N, Samire P, Aleksandrov A, Antonucci L, Benachir A, Boutet S, Byrdin M, Cammarata M, Carbajo S, Cuine S, Doak RB, Foucar L, Gorel A, Grunbein M, Hartmann E, Hienerwadel R, Hilpert M, Kloos M, Lane TJ, Legeret B, Legrand P, Li-Beisson Y, Moulin SLY, Nurizzo D, Peltier G, Schiro G, Shoeman RL, Sliwa M, Solinas X, Zhuang B, Barends TRM, Colletier JP, Joffre M, Royant A, Berthomieu C, Weik M, Domratcheva T, Brettel K, Vos MH, Schlichting I, Arnoux P, Muller P, Beisson F Science. 2021 Apr 9;372(6538). pii: 372/6538/eabd5687. doi:, 10.1126/science.abd5687. PMID:33833098<ref>PMID:33833098</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6yrx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Chlorella variabilis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arnoux P]] | [[Category: Arnoux P]] | ||
Current revision
Low-dose crystal structure of FAP at room temperature
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