6aaa
From Proteopedia
(Difference between revisions)
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<StructureSection load='6aaa' size='340' side='right' caption='[[6aaa]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6aaa' size='340' side='right' caption='[[6aaa]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6aaa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AAA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6aaa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amydetes Amydetes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AAA FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Photinus-luciferin_4-monooxygenase_(ATP-hydrolyzing) Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.7 1.13.12.7] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Photinus-luciferin_4-monooxygenase_(ATP-hydrolyzing) Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.7 1.13.12.7] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aaa OCA], [http://pdbe.org/6aaa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aaa RCSB], [http://www.ebi.ac.uk/pdbsum/6aaa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aaa ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aaa OCA], [http://pdbe.org/6aaa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aaa RCSB], [http://www.ebi.ac.uk/pdbsum/6aaa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aaa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:30456363</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6aaa" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Amydetes]] | ||
[[Category: Carrasco-Lopez, C]] | [[Category: Carrasco-Lopez, C]] | ||
[[Category: Naumov, P]] | [[Category: Naumov, P]] |
Revision as of 07:01, 5 December 2018
Structure of a blue-shifted Luciferase from Amydetes vivianii
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