6ABH
Structure of a natural red emitting luciferase from Phrixothrix hirtus (P1 crystal form)
Summary for 6ABH
Entry DOI | 10.2210/pdb6abh/pdb |
Related | 6AAA |
Descriptor | Red-bioluminescence eliciting luciferase (1 entity in total) |
Functional Keywords | bioluminescence, luciferase, red emission, luminescent protein |
Biological source | Phrixothrix hirtus |
Total number of polymer chains | 8 |
Total formula weight | 486665.72 |
Authors | Carrasco-Lopez, C.,Panjikar, S.,Naumov, P.,Rabeh, W. (deposition date: 2018-07-21, release date: 2018-08-22, Last modification date: 2023-11-22) |
Primary citation | Carrasco-Lopez, C.,Ferreira, J.C.,Lui, N.M.,Schramm, S.,Berraud-Pache, R.,Navizet, I.,Panjikar, S.,Naumov, P.,Rabeh, W.M. Beetle luciferases with naturally red- and blue-shifted emission. Life Sci Alliance, 1:e201800072-e201800072, 2018 Cited by PubMed Abstract: 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 is monomeric with a structural fold similar to the previously reported firefly luciferases. The only known naturally red-emitting luciferase from the glow-worm 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. PubMed: 30456363DOI: 10.26508/lsa.201800072 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.05 Å) |
Structure validation
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