Extended Data Fig. 7: Comparison of V-161 binding site of EhV-ATPase with the corresponding sites of other V- and F-ATPases.
From: Na+-V-ATPase inhibitor curbs VRE growth and unveils Na+ pathway structure
(a–d) Detailed views of the V-161 binding site of EhV-ATPase (a,b) and the corresponding site of F-ATPase (PDB ID: 6RDC) from Polytomella sp. Pringsheim (c,d), viewed as in Figs. 4i, j. (e) Sequence alignment of the c-subunit and the a-subunit from various V-ATPases (Na+-transporting types: from E. hirae and E. faecium; H+-transporting types: from rat and yeast) and F-ATPases (Na+-transporting types: from I. tartaricus and P. modestum; H+-transporting types: from bovine mitochondria (PDB ID: 6ZQM), yeast mitochondria (PDB ID: 6B8H), and Polytomella sp. Pringsheim (PDB ID: 6RDC)). Box colours adhere to the scheme in Fig. 3g. Residue numbers for E. hirae and Polytomella sp. Pringsheim are provided above and below the alignment, respectively. The residues c-T140 and a-N615 of Na+-transporting V-ATPase (shown in red boxes) are not conserved in other ATPases.
