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Crystallization and preliminary X-ray crystallographic studies of a PduO-type ATP : cob(I) alamin adenosyltransferase from Bacillus cereus

Authors
Park, Ae KyungMoon, Jin HoLee, Sung HaengChi, Young Min
Issue Date
7월-2008
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
Adenosylcobalamin; Adenosyltransferases; Cobalamins; MgATP
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.64, pp.648 - 650
Indexed
SCIE
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
64
Start Page
648
End Page
650
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/123074
DOI
10.1107/S1744309108016552
ISSN
2053-230X
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 angstrom resolution for the native crystals and 2.0 angstrom 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 angstrom. The asymmetric unit contained one trimer, with a corresponding V-M of 2.69 angstrom(3) Da(-1).
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생명과학대학 (생명공학부)
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