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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Archaeal Proteins / biosynthesis
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Cloning, Molecular
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Coenzymes / biosynthesis
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Coenzymes / chemistry
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Coenzymes / genetics
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins / metabolism
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Genes, Archaeal
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Hydrogen Bonding
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Metalloproteins / biosynthesis
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Metalloproteins / chemistry
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Metalloproteins / genetics
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Models, Molecular
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Molybdenum Cofactors
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Protein Conformation
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Protein Structure, Quaternary
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Protein Subunits
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Pteridines / chemistry
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Sulfolobus / chemistry*
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Sulfolobus / genetics
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Sulfolobus / metabolism
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Sulfurtransferases / metabolism
Substances
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Archaeal Proteins
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Coenzymes
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Escherichia coli Proteins
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Metalloproteins
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MoaB protein, E coli
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MoaC protein, E coli
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Molybdenum Cofactors
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Protein Subunits
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Pteridines
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Recombinant Proteins
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molybdenum cofactor
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Sulfurtransferases
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molybdopterin synthase