Structure of a putative molybdenum-cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472).
The crystal structure of a putative molybdenum-cofactor (Moco) biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472) was determined at 2.2 A resolution. The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 123.31, b = 78.58, c = 112.67 A, beta = 118.1 degrees . The structure was solved by molecular replacement using the structure of Escherichia coli MoaC as the probe model. The asymmetric unit is composed of a hexamer arranged as a trimer of dimers with noncrystallographic 32 symmetry. The structure of ST0472 is very similar to that of E. coli MoaC; however, in the ST0472 protein an additional loop formed by the insertion of seven residues participates in intermonomer interactions and the new structure also reveals the formation of an interdimer beta-sheet. These features may contribute to the stability of the oligomeric state.
Yoshida
Hiromi
H
Division of Structural Biology, Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
Yamada
Mitsugu
M
Kuramitsu
Seiki
S
Kamitori
Shigehiro
S
D000595:Amino Acid Sequence; D003067:Coenzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019281:Dimerization; D004795:Enzyme Stability / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D000090006:Molybdenum Cofactors; D017433:Protein Structure, Secondary; D011621:Pteridines / Q000737:chemistry* / Q000378:metabolism; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics
D003067:Coenzymes; D029968:Escherichia coli Proteins; D008667:Metalloproteins; D000090006:Molybdenum Cofactors; D011621:Pteridines; C413929:MoaC protein, E coli; C022261:molybdopterin