Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-ray structure of mutant W4L/R5S.
The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was solved by direct methods. The model of the air-oxidized protein was refined by partially restrained full-matrix least-squares refinement against intensity data to 0.69 A resolution. This first ultrahigh-resolution structure of a rubredoxin provides very detailed and precise information about the Fe(SCys)(4) centre and its environment, the peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and dynamic disorder, the solvent structure and the electron-density distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of mutants studied by atomic and ultrahigh-resolution X-ray crystallography which are expected to contribute to the understanding of structure-function relationships in iron-sulfur proteins.
Karolinska Institutet, Department of Biosciences at NOVUM, Center for Structural Biochemistry, Hälsovägen 7-9, S-14157 Huddinge, Sweden. heiko.bonisch@csb.ki.se
Heiko
H
Bönisch
Christian L
CL
Schmidt
Pierre
P
Bianco
Rudolf
R
Ladenstein
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray / Q000379:methods*; D004578:Electron Spin Resonance Spectroscopy; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010084:Oxidation-Reduction; D017354:Point Mutation; D043903:Pyrococcus abyssi / Q000737:chemistry*; D012416:Rubredoxins / Q000737:chemistry* / Q000235:genetics; D015204:Spectroscopy, Mossbauer; D013696:Temperature
D012416:Rubredoxins