Crystal structure of activated ModE reveals conformational changes involving both oxyanion and DNA-binding domains

Alexander W. Schuttelkopf, David H. Boxer, William N. Hunter

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)

    Abstract

    ModE is a bacterial transcriptional regulator that orchestrates many aspects of molybdenum metabolism by binding to specific DNA sequences in a molybdate-dependent fashion. We present the crystal structure of Escherichia coli ModE in complex with molybdate, which was determined at 2.75 Å from a merohedrally twinned crystal (twin fraction˜0.30) with space group P43. We now have structures of ModE in both its “switched on” (ligand-bound) and “switched off” (apo) states. Comparison with the apo structure shows that ligand binding leads to extensive conformational changes not only in the molybdate-binding domain, but also in the DNA-binding domain. The most obvious difference is the loss of the pronounced asymmetry between the two chains of the ModE dimer, which had been a characteristic property of the apo structure. Another major change concerns the relative orientation of the two DNA-interacting winged helix-turn-helix motifs. Manual docking of an idealized DNA structure suggests that this conformational change should improve DNA binding of the activated molybdate-bound ModE.
    Original languageEnglish
    Pages (from-to)761-767
    Number of pages7
    JournalJournal of Molecular Biology
    Volume326
    Issue number3
    DOIs
    Publication statusPublished - 2003

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