Details

Autor(en) / Beteiligte

• Tomabechi, Yuri
• Hosoya, Takamitsu
• Ehara, Haruhiko
• Sekine, Shun-ichi
• Shirouzu, Mikako
• Inouye, Satoshi

Titel

Crystal structure of nanoKAZ: The mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine

Ist Teil von

• Biochemical and biophysical research communications, 2016-01, Vol.470 (1), p.88-93

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2016

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 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 Å resolution. The structure consists of 11 antiparallel β-strands forming a β-barrel that is capped by 4 short α-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 β-barrel structure. •The 19 kDa protein (KAZ) of Oplophorus luciferase is a catalytic component.•The crystal structure of a mutant KAZ (nanoKAZ) was determined.•The structure consists of 11 β-strands and 4 α-helices, forming a β-barrel.•The structure of nanoKAZ is similar to those of fatty acid-binding proteins.•The coelenterazine-binding site might be in a central cavity of the protein.