Publication Abstract from PubMed
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.
Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.,Kim S, Suga M, Ogasahara K, Ikegami T, Minami Y, Yubisui T, Tsukihara T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):274-9. Epub 2007 Mar 23. PMID:17401193[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
