Adenosine diphosphate moiety does not participate in structural changes for the signaling state in the sensor of blue-light using FAD domain of AppA.
A sensor of blue light using FAD (BLUF) protein is a flavin adenine dinucleotide (FAD) based new class blue-light sensory flavoprotein. The BLUF domain of AppA was reconstituted in vitro from apoprotein and flavin adenine dinucleotide, flavin adenine mononucleotide or riboflavin. The light-induced FTIR spectra of the domain reconstituted from various flavins and the 13C-labeled apoprotein showed that identical light-induced structural changes occur in both the flavin chromophore and protein for the signaling state in all of the reconstituted holoproteins. The results showed that an adenosine 5'-dinucleotide moiety is not required for signaling-state formation in a BLUF domain.
Masuda
Shinji
S
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-5801, Japan. shmasuda@bio.titech.ac.jp
Hasegawa
Koji
K
Ono
Taka-Aki
TA
D000244:Adenosine Diphosphate / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry*; D005420:Flavoproteins / Q000737:chemistry*; D008027:Light; D017434:Protein Structure, Tertiary / Q000528:radiation effects; D015398:Signal Transduction; D017550:Spectroscopy, Fourier Transform Infrared; D014466:Ultraviolet Rays
C116785:AppA protein, Rhodobacter sphaeroides; D001426:Bacterial Proteins; D005420:Flavoproteins; D005182:Flavin-Adenine Dinucleotide; D000244:Adenosine Diphosphate