caa a22 4500 397557035 CHVBK 20180308164805.0 cr unu---uuuuu 161202e199607 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021376 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021376 Three-Dimensional Structure of Porcine Kidney D-Amino Acid Oxidase at 3.0 Å Resolution [Elektronische Daten] [Hisashi Mizutani, Ikuko Miyahara, Ken Hirotsu, Yasuzo Nishina, Kiyoshi Shiga, Chiaki Setoyama, Retsu Miura] The X-ray crystallographic structure of porcine kidney D-amino acid oxidase, which had been expressed in Escherichia coli transformed with a vector containing DAO cDNA, was determined by the isomorphous replacement method for the complex form with benzoate. The known amino acid sequence, FAD and benzoate were fitted to an electron density map of 3.0 Å resolution with an R-factor of 21.0%. The overall dimeric structure exhibits an elongated ellipsoidal framework. The prosthetic group, FAD, was found to be in an extended conformation, the isoalloxazine ring being buried in the protein core. The ADP moiety of FAD was located in the typical βαβ dinucleotide binding motif, with the α-helix dipole stabilizing the pyrophosphate negative charge. The substrate analog, benzoate, is located on the re-face of the isoalloxazine ring, while the si-face is blocked by hydrophobic residues. The carboxylate group of benzoate is ion-paired with the Arg283 side chain and is within interacting distance with the hydroxy moiety of Tyr228. The phenol ring of Tyr224 is located just above the benzene ring of benzoate, implying the importance of this residue for catalysis. There is no positive charge or α-helix dipole near N(1) of flavin. Hydrogen bonds were observed at C(2)=O, N(3)-H, C(4)=O, and N(5) of the flavin ring. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Rapid Communications nationallicence D-amino acid oxidase nationallicence enzyme-ligand interaction nationallicence flavoenzyme nationallicence three dimensional structure nationallicence X-ray crystallography nationallicence Mizutani Hisashi Department of Chemistry, Faculty of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka 558 aut Miyahara Ikuko Department of Chemistry, Faculty of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka 558 aut Hirotsu Ken Department of Chemistry, Faculty of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka 558 aut Nishina Yasuzo Departments of Physiology, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut Shiga Kiyoshi Departments of Physiology, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut Setoyama Chiaki Departments of Biochemistry, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut Miura Retsu Departments of Biochemistry, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut The Journal of Biochemistry Oxford University Press 120/1(1996-07), 14-17 0021-924X 120:1<14 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021376 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021376 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Mizutani Hisashi Department of Chemistry, Faculty of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka 558 aut NATIONALLICENCE 700 1- Miyahara Ikuko Department of Chemistry, Faculty of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka 558 aut NATIONALLICENCE 700 1- Hirotsu Ken Department of Chemistry, Faculty of Science, Osaka City University Sugimoto, Sumiyoshi-ku, Osaka 558 aut NATIONALLICENCE 700 1- Nishina Yasuzo Departments of Physiology, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut NATIONALLICENCE 700 1- Shiga Kiyoshi Departments of Physiology, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut NATIONALLICENCE 700 1- Setoyama Chiaki Departments of Biochemistry, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut NATIONALLICENCE 700 1- Miura Retsu Departments of Biochemistry, Kumamoto University School of Medicine Honjo, Kumamoto 860 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/1(1996-07), 14-17 0021-924X 120:1<14 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford