AI Article Synopsis
- The crystal structure of a mutant rubredoxin from Pyrococcus abyssi (W4L/R5S) was determined using direct methods and refined to ultra-high resolution (0.69 A).
- This study provided detailed insights into the iron center, peptide stereochemistry, hydrogen bonds, and the surrounding environment of the protein.
- The research is part of a series of studies on mutants aimed at enhancing our understanding of the relationship between structure and function in iron-sulfur proteins.
Article Abstract
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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1107/S090744490501293X | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Interpretation of nuclear resonant vibrational spectra of rubredoxin using a combined quantum mechanics and molecular mechanics approach.
Chemphyschem
December 2011
Institut für Physik, Universität zu Lübeck, 23562 Lübeck, Germany.
Nuclear resonant vibrational spectra of the reduced and oxidized form of a mutant of rubredoxin from Pyrococcus abyssii were measured and are compared with simulated spectra that were calculated by a combined quantum mechanics (QM) and molecular mechanics (MM) method. Density functional theory was used for the QM level. Calculations were performed for different models of rubredoxin.
View Article and Find Full Text PDFUltrahigh-resolution study on Pyrococcus abyssi rubredoxin: II. Introduction of an O-H...Sgamma-Fe hydrogen bond increased the reduction potential by 65 mV.
J Biol Inorg Chem
November 2007
Center of Biosciences, Karolinska Institutet, Hälsovägen 7-9, Huddinge, Sweden.
The effect of D-H...
View Article and Find Full Text PDFUltrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-ray structure of mutant W4L/R5S.
Acta Crystallogr D Biol Crystallogr
July 2005
Karolinska Institutet, Department of Biosciences at NOVUM, Center for Structural Biochemistry, Hälsovägen 7-9, S-14157 Huddinge, Sweden.
Article Synopsis
- The crystal structure of a mutant rubredoxin from Pyrococcus abyssi (W4L/R5S) was determined using direct methods and refined to ultra-high resolution (0.69 A).
- This study provided detailed insights into the iron center, peptide stereochemistry, hydrogen bonds, and the surrounding environment of the protein.
- The research is part of a series of studies on mutants aimed at enhancing our understanding of the relationship between structure and function in iron-sulfur proteins.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!