Abstract
The structure of a probable Mo-cofactor biosynthesis protein B from Sulfolobus tokodaii, belonging to space group P6422 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. © 2009 International Union of Crystallography All rights reserved.
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Antonyuk, S. V., Strange, R. W., Ellis, M. J., Bessho, Y., Kuramitsu, S., Shinkai, A., … Hasnain, S. S. (2009). Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from Sulfolobus tokodaii. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(12), 1200–1203. https://doi.org/10.1107/S1744309109043772
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