title: Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from Sulfolobus tokodaii.
abstract: The structure of a probable Mo-cofactor biosynthesis protein B from Sulfolobus tokodaii, belonging to space group P6(4)22 with unit-cell parameters a = b = 136.68, c = 210.52 A, was solved by molecular replacement to a resolution of 1.9 A 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.
authors.affiliation: Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, England.
authors.forename: Svetlana V
authors.initials: SV
authors.lastname: Antonyuk
authors.forename: Richard W
authors.initials: RW
authors.lastname: Strange
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Ellis
authors.forename: Yoshitaka
authors.initials: Y
authors.lastname: Bessho
authors.forename: Seiki
authors.initials: S
authors.lastname: Kuramitsu
authors.forename: Akeo
authors.initials: A
authors.lastname: Shinkai
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
authors.forename: S Samar
authors.initials: SS
authors.lastname: Hasnain
mesh_terms: D019843:Archaeal Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D003067:Coenzymes / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D019766:Genes, Archaeal; D006860:Hydrogen Bonding; D008667:Metalloproteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D008958:Models, Molecular; D000090006:Molybdenum Cofactors; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D011621:Pteridines / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D016944:Sulfolobus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013466:Sulfurtransferases / Q000378:metabolism
chemical_list: D019843:Archaeal Proteins; D003067:Coenzymes; D029968:Escherichia coli Proteins; D008667:Metalloproteins; D000090006:Molybdenum Cofactors; D021122:Protein Subunits; D011621:Pteridines; D011994:Recombinant Proteins; D013466:Sulfurtransferases; C492989:MoaB protein, E coli; C413929:MoaC protein, E coli; C022261:molybdopterin; C085585:molybdopterin synthase