CAVER 3.0: A Tool for the Analysis of Transport Pathways in Dynamic Protein Structures
Figure 5
Bottleneck dynamics and structural basis of gating in the p1 tunnel of DhaA.
(A) The bottleneck 1 represents the most frequent bottleneck of the p1 tunnel and is mostly formed by Ala145, Phe149, Ala172 and Cys176. Comparison of snapshots with an open (red) and closed (blue) p1 tunnels suggested that the gating is mediated by: (i) movement of the N-terminal part of the cap domain carrying Ala145 and Phe149; (ii) movement of the α5-helix with Cys176 and Ala172; and (iii) conformational change of the bottleneck residues Phe149 and Cys176. The bottleneck radius in the selected snapshots with an open and closed tunnel was 2.3 Å and 0.9 Å, respectively. (B) The bottleneck 2 of the p1 tunnel is mostly formed by Thr148, Ala172 and Lys175. Comparison of snapshots with an open (red) and closed (green) p1 tunnel suggested that gating is mediated by: (i) movement of the N-terminal part of the cap domain carrying Thr148; (ii) movement of the α5-helix carrying Ala172; and (iii) the conformational change of the bottleneck residues Thr148 and Lys175. The bottleneck radius in the selected snapshot with an open and closed tunnel was 2.3 Å and 0.9 Å, respectively.