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. 2013 Apr 15;288(22):15800–15812. doi: 10.1074/jbc.M113.462440

TABLE 2.

Properties of AcnR derivatives used

Mutation Location Further information
pEKEx2-AcnR-STREP derivatives
    K43A DBD Almost complete abolishment of DNA binding
    K55A DBD Complete abolishment of DNA binding
    K104A Dimer interface DNA affinity close to wild-type protein
    E65A Beginning of α4 Maybe involved in signal transduction to the DNA binding domain, no effect on DNA binding
    D66A Beginning of α4 Maybe involved in signal transduction to the DNA binding domain, no effect on DNA binding
    R99A P pocket Weaker binding to DNA
    D109A Protein surface No effect on DNA binding
    R130A D pocket Hydrogen-bonds to citrate, does not change its affinity to DNA in the presence of citrate-Mg2+
    R141A Protein surface No effect on DNA binding
    D143A Protein surface No effect on DNA binding
    D158A P pocket Weaker binding to DNA
    E181A D pocket Binds Mg ion, does not change its affinity to DNA in the presence of citrate-Mg2+
    R185A D pocket Hydrogen-bonds to citrate, does not change its affinity to DNA in the presence of citrate-Mg2+

pET-TEV-AcnR derivatives
    C23A Within α1 No obvious difference in behavior,
    R69A P pocket No obvious difference in behavior
    M70A P pocket No obvious difference in behavior
    M86A P pocket No obvious difference in behavior
    R92A P pocket No obvious difference in behavior
    W95A P pocket No obvious difference in behavior
    R130A D pocket Does not change its affinity to DNA in the presence of citrate-Mg2+