5b0u: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/LUCI_OPLGR LUCI_OPLGR]] Catalytic subunit of oplophorus-luciferin 2-monooxygenase. Oxidoreductase that converts coelenterazine (the oplophorus luciferin) to coelenteramide under emission of blue light with a maximum at 454 nm. Is also active with bisdeoxycoelenterazine.<ref>PMID:10984608</ref> | [[http://www.uniprot.org/uniprot/LUCI_OPLGR LUCI_OPLGR]] Catalytic subunit of oplophorus-luciferin 2-monooxygenase. Oxidoreductase that converts coelenterazine (the oplophorus luciferin) to coelenteramide under emission of blue light with a maximum at 454 nm. Is also active with bisdeoxycoelenterazine.<ref>PMID:10984608</ref> | ||
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== Publication Abstract from PubMed == | |||
The 19 kDa protein (KAZ) of Oplophorus luciferase is a catalytic component, that oxidizes coelenterazine (a luciferin) with molecular oxygen to emit light. The crystal structure of the mutated 19 kDa protein (nanoKAZ) was determined at 1.71 A resolution. The structure consists of 11 antiparallel beta-strands forming a beta-barrel that is capped by 4 short alpha-helices. The structure of nanoKAZ is similar to those of fatty acid-binding proteins (FABPs), even though the amino acid sequence similarity was very low between them. The coelenterazine-binding site and the catalytic site for the luminescence reaction might be in a central cavity of the beta-barrel structure. | |||
Crystal structure of nanoKAZ: The mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine.,Tomabechi Y, Hosoya T, Ehara H, Sekine S, Shirouzu M, Inouye S Biochem Biophys Res Commun. 2016 Jan 29;470(1):88-93. doi:, 10.1016/j.bbrc.2015.12.123. Epub 2015 Dec 30. PMID:26746005<ref>PMID:26746005</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
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