Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP

Ae Kyung Park, Young Min Chi, Jin Ho Moon

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    ATP:Cobalamin adenosyltransferases catalyze the transfer a 5′-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12. There are three types of adenosyltransferases, CobA, PduO and EutT. Among these adenosyltransferases, the PduO-type adenosyltransferases is the most widely distributed enzyme. Structural comparisons between apo BcPduO and BcPduO in complex with MgATP revealed that the N-terminal strands of both structures were ordered, which is in contrast with the most previously available PduO-type adenosyltransferase structures. Furthermore, unlike other reported structures, apo BcPduO was bound to additional dioxane molecules causing a side chain conformational change at the Tyr30 residue, which is an important residue that mediates hydrogen bonding with ATP molecules upon binding of cobalamin to the active site. This study provides more structural information into the role of active site residues on substrate binding.

    Original languageEnglish
    Pages (from-to)417-421
    Number of pages5
    JournalBiochemical and biophysical research communications
    Volume408
    Issue number3
    DOIs
    Publication statusPublished - 2011 May 13

    Bibliographical note

    Funding Information:
    We thank the staff at beamline 6C of Pohang Light Source, South Korea, for assistance during the data collection. This work was supported by a Korea University Grant.

    Keywords

    • Adenosylcobalamin
    • Adenosyltransferase
    • Cobalamin
    • MgATP
    • PduO

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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