title: Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.
abstract: 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.
authors.affiliation: Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka, Japan.
authors.forename: Sangwoo
authors.initials: S
authors.lastname: Kim
authors.forename: Michihiro
authors.initials: M
authors.lastname: Suga
authors.forename: Kyoko
authors.initials: K
authors.lastname: Ogasahara
authors.forename: Terumi
authors.initials: T
authors.lastname: Ikegami
authors.forename: Yoshiko
authors.initials: Y
authors.lastname: Minami
authors.forename: Toshitsugu
authors.initials: T
authors.lastname: Yubisui
authors.forename: Tomitake
authors.initials: T
authors.lastname: Tsukihara
mesh_terms: 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
chemical_list: D005182:Flavin-Adenine Dinucleotide; D015786:Cytochromes b5