Luciferase
Luciferase (Luc) is an oxidative enzyme used in bioluminescence. It catalyzes the oxidation of the pigment luciferin producing oxyluciferin and light. The images at the left and at the right correspond to one representative Luc, i.e. the crystal structure of firefly Luciferase (3iep).
3D Structures of Luciferase3D Structures of Luciferase
3iep, 1lci – fLuc – firefly
3ier – fLuc+PEG 400
1ba3 – fLuc+bromoform
3ies – fLuc+inhibitor
2d1q – LcLuc (mutant)+MgATP – Luciola cruciata
2d1r - LcLuc (mutant)+oxyluciferin+AMP
2d1s, 2d1t - LcLuc (mutant)+intermediate analog
3fgc – VhLuc α+β chain+FMN – Vibrio harveyi
1luc, 1brl - VhLuc α+β chain
1bsl, 1xkj - VhLuc β chain
2psd, 2psh, 2psj, 2pse, 2psf – Luc (mutant) – Renilla reniformis
Additional informationAdditional information
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Several organisms are bioluminescent, meaning that they produce light. Luciferase is one of the enzymes that catalyzes light emitting reactions in organisms.
- Luciola cruciata luciferase (Japanese firefly), complexed with Oxyluciferin & AMP (2d1r) or with an high-energy analogue (2d1s)
- 3ies,3iep and 3ier Firefly luciferase (FLuc) bound to its natural substrate ATP and the inhibitor PTC124[1]
- 1ba3 firefly luciferase enzyme from Photinus pyralis
- 2psd, 2pse, 2psf, 2psh, 2psj, and 2rh7 the luciferase from Renilla reniformis (RLuc)
- 1bsl 1.95Å heterodimer of bacterial luciferase from Vibrio harveyi
- 1brl 2.4Å heterodimer of bacterial luciferase from Vibrio harveyi
- 1xkj homodimer of bacterial luciferase from Vibrio harveyi
- 2d1q, 2d1r and 2d1s thermostable Japanese Firefly (Luciola cruciata) Luciferase complexed with High-energy intermediate analog
- 2d1t thermostable Japanese Firefly Luciferase red-color emission S286N mutant
- 1lci firefly luciferase enzyme from Photinus pyralis
- Dinoflagellate luciferase
- 1luc The 1.5Å resolution crystal structure of bacterial luciferase from Vibrio harveyi
- 3fgc Bacterial luciferase from Vibrio harveyi[2]
- 1vpr luciferase of Lingulodinium polyedrum, a marine bioluminescent dinoflagellate
- Green Fluorescent Protein
- For additional information, see: Colored & Bioluminescent Proteins
ReferencesReferences
- ↑ Auld DS, Lovell S, Thorne N, Lea WA, Maloney DJ, Shen M, Rai G, Battaile KP, Thomas CJ, Simeonov A, Hanzlik RP, Inglese J. Molecular basis for the high-affinity binding and stabilization of firefly luciferase by PTC124. Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):4878-83. Epub 2010 Mar 1. PMID:20194791
- ↑ Campbell ZT, Weichsel A, Montfort WR, Baldwin TO. Crystal Structure of the Bacterial Luciferase:Flavin Complex Provides Insight into the Function of the subunit. Biochemistry. 2009 May 12. PMID:19435287 doi:http://dx.doi.org/10.1021/bi900003t
Additional LiteratureAdditional Literature
- ↑ Marques SM, Esteves da Silva JC. Firefly bioluminescence: a mechanistic approach of luciferase catalyzed reactions. IUBMB Life. 2009 Jan;61(1):6-17. PMID:18949818 doi:10.1002/iub.134
- ↑ Inouye S. Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions. Cell Mol Life Sci. 2010 Feb;67(3):387-404. Epub 2009 Oct 27. PMID:19859663 doi:10.1007/s00018-009-0170-8
External ResourcesExternal Resources
- Yahoo news coverage of luciferase studies funded research for military applications
- Luciferase at Wikipedia
- Luciferase: June 2006 Molecule of the Month as part of the series of tutorials that are at the RCSB Protein Data Bank and written by David S. Goodsell