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. Author manuscript; available in PMC: 2015 Dec 18.
Published in final edited form as: J Biol Chem. 2005 Feb 14;280(15):14611–14619. doi: 10.1074/jbc.M414224200

FIG. 3. High-affinity binding of two ATP molecules per SecA dimer.

FIG. 3

Membrane filtration experiments performed with 2.5 μM SecA dimer reveal that the wild type (WT) SecA (A) as well as SecA-E210D (B) and SecA-E210N (C) bind two ATP molecules per dimer with high affinity; apparent Kd 1.5 ± 0.3, 2.4 ± 0.8, 0.8 ± 0.1 M, respectively (nonspecific ATP binding to the membrane is negligible (◆)).