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Figure 1

From: Mutant LV476-7AA of A-subunit of Enterococcus hirae V1-ATPase: High affinity of A3B3 complex to DF axis and low ATPase activity

Figure 1

Positions of the critical contact residues of A- and/or B-subunits with DF complex in the structure of E. hirae V 1 -ATPase (Arai et al. 2013 ; Saijo et al. 2011 ). (A) The side-viewed ribbon representation of the “tight” form of A- (tv_blue) and B-subunit (violet) together with DF (tv_green and firebrick, respectively) complex. Spheres (in red circle) indicate the selected residues (Figure 1B-E) for mutation of the corresponding subunits. (B) The closer view of the critical contact residue LV476-7 (tv_blue spheres) of the A-subunit with DF complex. (C) The closer view of the critical contact residues (LV476-7 (tv_blue spheres) of A-subunit and L389 (violet spheres) of B-subunit) of the “tight” form of A- and B-subunits together with DF complex. (D) The closer view of the “tight” form of A-subunit together with DF complex showing the critical contact residues; LV476-7 (tv_blue spheres) of A-subunit and RR165-6 (tv_green spheres) of D-subunit. (E) The closer view of the “tight” form of A-subunit together with DF complex showing the critical contact residues; LV476-7 (tv_blue spheres) of A-subunit and L170 (tv_green spheres) of D-subunit. (F) The “tight” form of A-subunit (tv_blue) together with DF (tv_green and firebrick, respectively) complex showing the 480DSLSDND486 sequence of A-subunit (yellow in red circle), probably corresponding to the DELSEED sequence of F-ATPase (Mnatsakanyan et al. 2011; Nakanishi-Matsui & Futai 2008).

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