Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum.
Crystals of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum diffract X-rays to 0.80 A using synchrotron radiation at 100 K. The crystal structure of this HiPIP was refined at this ultrahigh resolution with anisotropic temperature factors for all atoms to conventional crystallographic R factors of 0.092 and 0.101 for F(o) > 4sigma(F(o)) and all reflections, respectively. The present structure provides a more precise picture than the previous 1.5 A structure and allows location of the positions of most H atoms. The structure revealed a partly hydrophobic cavity near the main hydrophobic area and a much larger inter-cluster approach distance (23.454 A, the c constant of the unit cell) in the crystal packing than other types of HiPIPs. The structural features involved in the electron-transfer reaction of HiPIP are discussed.
Liu
Lijun
L
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Japan.
Nogi
Terukazu
T
Kobayashi
Masayuki
M
Nozawa
Tsunenori
T
Miki
Kunio
K
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002841:Chromatiaceae / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods*; D004583:Electrons; D006860:Hydrogen Bonding; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008958:Models, Molecular; D013696:Temperature
D007506:Iron-Sulfur Proteins