1ba3
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FIREFLY LUCIFERASE IN COMPLEX WITH BROMOFORM
OverviewOverview
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.
About this StructureAbout this Structure
1BA3 is a Single protein structure of sequence from Photinus pyralis with MBR as ligand. Active as Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7 Full crystallographic information is available from OCA.
ReferenceReference
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
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