Figure 1.
The Structures Related to AChE Tetramerization
(A) The [WAT]4PRAD complex structure. (B) The compact tetramer structure. (C) The loose tetramer structure. (D) The [AChET]4–ColQ complex model constructed according to the [WAT]4PRAD complex structure. Each chain is colored differently (A, blue; B, red; C, gray; D, orange; ColQ, yellow). The catalytic S203 was shown as a green ball model for each AChE subunit, and the cyan surfaces are residues near the peripheral site.
Figure 2.
The RMSF of the [AChET]4–ColQ Complex as Calculated from the 100 Lowest Frequency Modes
All residues are numbered continuously (chain A: 1–583, B: 584-1166, C: 1167–1749, D: 1750–2332, ColQ: 2333–2379).
Figure 3.
The Motion Correlation Map of the [AChET]4–ColQ Complex as Predicted by BNMA
Only one AChE subunit and ColQ were plotted here (AChE: 1–583, ColQ: 584–630).
Figure 4.
The Involvement Analysis of the Low-Frequency Modes of the [AChET]4–ColQ Complex
The involvement of the modes was shown for the conformational change to (A) the compact and (B) loose tetramer structures. The cumulative involvement of the modes was shown for (C) the compact and (D) loose tetramer structures.
Figure 5.
Illustration of Motions in the Two Lowest Frequency Modes from BNMA
The arrow represents the amplitude and direction of the displacement experienced by each residue in the conformational change. Frequencies of the two modes are (A) 1.49 cm−1 and (B) 1.66 cm−1.