FIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORMFIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORM

Structural highlights

1ba3 is a 1 chain structure with sequence from Photinus pyralis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LUCI_PHOPY Produces green light with a wavelength of 562 nm.

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The firefly luciferase enzyme from Photinus pyralis is probably the best-characterized model system for studying anesthetic-protein interactions. It binds a diverse range of general anesthetics over a large potency range, displays a sensitivity to anesthetics that is very similar to that found in animals, and has an anesthetic sensitivity that can be modulated by one of its substrates (ATP). In this paper we describe the properties of bromoform acting as a general anesthetic (in Rana temporaria tadpoles) and as an inhibitor of the firefly luciferase enzyme at high and low ATP concentrations. In addition, we describe the crystal structure of the low-ATP form of the luciferase enzyme in the presence of bromoform at 2.2-A resolution. These results provide a structural basis for understanding the anesthetic inhibition of the enzyme, as well as an explanation for the ATP modulation of its anesthetic sensitivity.

Structural basis for the inhibition of firefly luciferase by a general anesthetic.,Franks NP, Jenkins A, Conti E, Lieb WR, Brick P Biophys J. 1998 Nov;75(5):2205-11. PMID:9788915[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Franks NP, Jenkins A, Conti E, Lieb WR, Brick P. Structural basis for the inhibition of firefly luciferase by a general anesthetic. Biophys J. 1998 Nov;75(5):2205-11. PMID:9788915

1ba3, resolution 2.20Å

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