title: Cyanidioschyzon merolae ferredoxin: a high resolution crystal structure analysis and its thermal stability.
abstract: Cyanidioschyzon merolae (Cm) is a single-cell red alga that grows under moderately thermophilic (40-50°C), acidic (pH 1-3) conditions. We purified a Cm ferredoxin (Fd) that was characterized as a plant-type [2Fe-2S] Fd by physicochemical techniques. X-ray crystallography revealed that the overall three-dimensional structure of CmFd was highly similar to, but slightly different from, the [2Fe-2S] Fd from Spinacia oleracea, whose growth temperature is 15-20°C. Therefore, slight structural differences, including non-covalent-bond number and amino acid sequence, may underlie the differential thermostabilities of the plant-type Fds.
authors: Department of Life Science and Graduate School of Life Science, Rikkyo (St. Paul's) University, Toshima-ku, Tokyo, Japan.
authors: Asami
authors: A
authors: Yamaoka
authors: Yukiko
authors: Y
authors: Ozawa
authors: Yuko
authors: Y
authors: Ueno
authors: Tsukasa
authors: T
authors: Endo
authors: Yukio
authors: Y
authors: Morimoto
authors: Akio
authors: A
authors: Urushiyama
authors: Daijiro
authors: D
authors: Ohmori
authors: Takeo
authors: T
authors: Imai
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D005288:Ferredoxins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D055550:Protein Stability; D011994:Recombinant Proteins / Q000737:chemistry* / Q000378:metabolism; D000461:Rhodophyta / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman; D013696:Temperature
chemical_list: C081714:2Fe-2S ferredoxin; D005288:Ferredoxins; D010940:Plant Proteins; D011994:Recombinant Proteins