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 Mg2+ and ATP (MgATP). Diffraction data were collected to 1.9 Å resolution for the native crystals and 2.0 Å resolution for the complexed crystals. Both crystals belonged to the orthorhombic space group C2221; the native crystals have unit-cell parameters a = 64.93, b = 137.08, c = 158.55 Å. The asymmetric unit contained one trimer, with a corresponding V M of 2.69 Å3 Da-1.
Original language | English |
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Pages (from-to) | 648-650 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 64 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2008 |
Keywords
- Adenosylcobalamin
- Adenosyltransferases
- Cobalamins
- MgATP
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics