Open AccessStructure of hypothetical Mo‐cofactor biosynthesis protein B (ST2315) from Sulfolobus tokodaii
Author(s) -
Antonyuk Svetlana V.,
Strange Richard W.,
Ellis Mark J.,
Bessho Yoshitaka,
Kuramitsu Seiki,
Shinkai Akeo,
Yokoyama Shigeyuki,
Hasnain S. Samar
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109043772
Subject(s) - trimer , random hexamer , cofactor , biosynthesis , molybdenum cofactor , sulfolobus , protein subunit , stereochemistry , chemistry , molecular replacement , biochemistry , enzyme , dimer , archaea , organic chemistry , gene
The structure of a probable Mo‐cofactor biosynthesis protein B from Sulfolobus tokodaii , belonging to space group P 6 4 22 with unit‐cell parameters a = b = 136.68, c = 210.52 Å, was solved by molecular replacement to a resolution of 1.9 Å and refined to an R factor and R free of 16.8% and 18.5%, respectively. The asymmetric unit contains a trimer, while the biologically significant oligomer is predicted to be a hexamer by size‐exclusion chromatography. The subunit structure and fold of ST2315 are similar to those of other enzymes that are known to be involved in the molybdopterin‐ and molybdenum cofactor‐biosynthesis pathways.