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Crystal structure of the mutated 19 kDa protein of Oplophorus luciferase (nanoKAZ)Crystal structure of the mutated 19 kDa protein of Oplophorus luciferase (nanoKAZ)
Structural highlights
Function[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.[1] Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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