Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.
Physarum polycephalum cytochrome b(5) reductase catalyzes the reduction of cytochrome b(5) by NADH. The structure of P. polycephalum cytochrome b(5) reductase was determined at a resolution of 1.56 A. The molecular structure was compared with that of human cytochrome b(5) reductase, which had previously been determined at 1.75 A resolution [Bando et al. (2004), Acta Cryst. D60, 1929-1934]. The high-resolution structure revealed conformational differences between the two enzymes in the adenosine moiety of the FAD, the lid region and the linker region. The structural properties of both proteins were inspected in terms of hydrogen bonding, ion pairs, accessible surface area and cavity volume. The differences in these structural properties between the two proteins were consistent with estimates of their thermostabilities obtained from differential scanning calorimetry data.
Kim
Sangwoo
S
Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka, Japan.
Suga
Michihiro
M
Ogasahara
Kyoko
K
Ikegami
Terumi
T
Minami
Yoshiko
Y
Yubisui
Toshitsugu
T
Tsukihara
Tomitake
T
D000818:Animals; D002152:Calorimetry, Differential Scanning; D018360:Crystallography, X-Ray; D015786:Cytochromes b5 / Q000737:chemistry* / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D006860:Hydrogen Bonding; D016839:Physarum polycephalum / Q000201:enzymology*; D011487:Protein Conformation
D005182:Flavin-Adenine Dinucleotide; D015786:Cytochromes b5