Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 Å resolution

Sangwoo Kim, Michihiro Suga, Kyoko Ogasahara, Terumi Ikegami, Yoshiko Minami, Toshitsugu Yubisui, Tomitake Tsukihara

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Physarum polycephalum cytochrome b5 reductase catalyzes the reduction of cytochrome b5 by NADH. The structure of P. polycephalum cytochrome b5 reductase was determined at a resolution of 1.56 Å. The molecular structure was compared with that of human cytochrome b5 reductase, which had previously been determined at 1.75 Å 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.

Original languageEnglish
Pages (from-to)274-279
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number4
DOIs
Publication statusPublished - Dec 1 2007
Externally publishedYes

Keywords

  • Cytochrome b reductase
  • Physarum polycephalum

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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