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| <StructureSection load='6abh' size='340' side='right'caption='[[6abh]], [[Resolution|resolution]] 3.05Å' scene=''> | | <StructureSection load='6abh' size='340' side='right'caption='[[6abh]], [[Resolution|resolution]] 3.05Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6abh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Phrixothrix_hirtus Phrixothrix hirtus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ABH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ABH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6abh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Phrixothrix_hirtus Phrixothrix hirtus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ABH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ABH FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6aaa|6aaa]]</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]] 3.05Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6abh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6abh OCA], [http://pdbe.org/6abh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6abh RCSB], [http://www.ebi.ac.uk/pdbsum/6abh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6abh ProSAT]</span></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=6abh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6abh OCA], [https://pdbe.org/6abh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6abh RCSB], [https://www.ebi.ac.uk/pdbsum/6abh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6abh ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q9U4U7_9COLE Q9U4U7_9COLE] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Phrixothrix hirtus]] | | [[Category: Phrixothrix hirtus]] |
- | [[Category: Carrasco-Lopez, C]] | + | [[Category: Carrasco-Lopez C]] |
- | [[Category: Naumov, P]] | + | [[Category: Naumov P]] |
- | [[Category: Panjikar, S]] | + | [[Category: Panjikar S]] |
- | [[Category: Rabeh, W]] | + | [[Category: Rabeh W]] |
- | [[Category: Bioluminescence]]
| + | |
- | [[Category: Luciferase]]
| + | |
- | [[Category: Luminescent protein]]
| + | |
- | [[Category: Red emission]]
| + | |
| Structural highlights
Function
Q9U4U7_9COLE
Publication Abstract from PubMed
The different colors of light emitted by bioluminescent beetles that use an identical substrate and chemiexcitation reaction sequence to generate light remain a challenging and controversial mechanistic conundrum. The crystal structures of two beetle luciferases with red- and blue-shifted light relative to the green yellow light of the common firefly species provide direct insight into the molecular origin of the bioluminescence color. The structure of a blue-shifted green-emitting luciferase from the firefly Amydetes vivianii is monomeric with a structural fold similar to the previously reported firefly luciferases. The only known naturally red-emitting luciferase from the glow-worm Phrixothrix hirtus exists as tetramers and octamers. Structural and computational analyses reveal varying aperture between the two domains enclosing the active site. Mutagenesis analysis identified two conserved loops that contribute to the color of the emitted light. These results are expected to advance comparative computational studies into the conformational landscape of the luciferase reaction sequence.
Beetle luciferases with naturally red- and blue-shifted emission.,Carrasco-Lopez C, Ferreira JC, Lui NM, Schramm S, Berraud-Pache R, Navizet I, Panjikar S, Naumov P, Rabeh WM Life Sci Alliance. 2018 Aug 16;1(4):e201800072. doi: 10.26508/lsa.201800072., eCollection 2018 Aug. PMID:30456363[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Carrasco-Lopez C, Ferreira JC, Lui NM, Schramm S, Berraud-Pache R, Navizet I, Panjikar S, Naumov P, Rabeh WM. Beetle luciferases with naturally red- and blue-shifted emission. Life Sci Alliance. 2018 Aug 16;1(4):e201800072. doi: 10.26508/lsa.201800072., eCollection 2018 Aug. PMID:30456363 doi:http://dx.doi.org/10.26508/lsa.201800072
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