Open AccessStructure of a putative molybdenum‐cofactor biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472)
Author(s) -
Yoshida Hiromi,
Yamada Mitsugu,
Kuramitsu Seiki,
Kamitori Shigehiro
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910801590x
Subject(s) - trimer , random hexamer , biology , cofactor , sulfolobus , sulfolobus acidocaldarius , molecular replacement , protein structure , crystallography , crystal structure , stereochemistry , biochemistry , archaea , chemistry , dimer , enzyme , gene , organic chemistry
The crystal structure of a putative molybdenum‐cofactor (Moco) biosynthesis protein C (MoaC) from Sulfolobus tokodaii (ST0472) was determined at 2.2 Å resolution. The crystal belongs to the monoclinic space group C 2, with unit‐cell parameters a = 123.31, b = 78.58, c = 112.67 Å, β = 118.1°. 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 β‐sheet. These features may contribute to the stability of the oligomeric state.