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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.

SUBMITTER: Antonyuk SV

PROVIDER: S-EPMC2802863 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from Sulfolobus tokodaii.

Antonyuk Svetlana V SV Strange Richard W RW Ellis Mark J MJ Bessho Yoshitaka Y Kuramitsu Seiki S Shinkai Akeo A Yokoyama Shigeyuki S Hasnain S Samar SS

Acta crystallographica. Section F, Structural biology and crystallization communications 20091127 Pt 12

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 a ...[more]

PMID: 20054111

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