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  • Title: Crystallization and preliminary X-ray crystallographic studies of a PduO-type ATP:cob(I)alamin adenosyltransferase from Bacillus cereus.
    Author: Park AK, Moon JH, Lee SH, Chi YM.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2008 Jul 01; 64(Pt 7):648-50. PubMed ID: 18607099.
    Abstract:
    Cobalamin adenosyltransferases transfer a 5'-deoxyadenosyl moiety from ATP and covalently attach it to the cobalt(I) ion of the corrin ring of cobalamin to generate adenosylcobalamin. The PduO-type adenosyltransferase from Bacillus cereus was overexpressed in Escherichia coli, purified and crystallized as the apoenzyme as well as in complex with Mg(2+) and ATP (MgATP). Diffraction data were collected to 1.9 A resolution for the native crystals and 2.0 A resolution for the complexed crystals. Both crystals belonged to the orthorhombic space group C222(1); the native crystals have unit-cell parameters a = 64.93, b = 137.08, c = 158.55 A. The asymmetric unit contained one trimer, with a corresponding V(M) of 2.69 A(3) Da(-1).
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