Mutational Data

FtsY

Thr446Asn- GTP-binding

Asp449Ala- GTP-binding

Ffh (E. coli = T.a. +2)

Gln108 and Leu194 sit on nitrogenase produced Ffh-FtsY interface, Leu194 inserts to other protein face

Ffh (A. ambivalens)

T112A mutant- won't hydrolyze the GTP, the loss of the polar -OH of Thr abolishes the interaction with Asp187 sc and H-bond formed by Gln107 and Arg138

Ffh (T. aquaticus)

Leu106 and Leu192 may contribute to protein interaction surface

Leu320, Phe325, Leu326, Met329, Leu362, Phe402, Met409 may contribute to the hydrophobic groove

Leu322, Ile365, Met369, Phe406 may form hydrophobic core of M-domain