 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](be5250fig4mag.jpg)
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Figure 4
Motion of protein loops during the exit of the citrate molecule from the binding site through the extracellular gate. The 1.9 Å resolution citrate-bound crystal structure with the T8 loop modelled in an ordered conformation was used in this simulation. Upper panel: time evolution of the root-mean-squared deviation of protein backbone atoms. The T8 and L2 loop regions are indicated. Coloured squares identify key motions of the protein. Lower panels: snapshots of citrate motion through the E-gate. The approximate location of the extracellular (E) and periplasmic (P) sides of the membrane are indicated. Coloured boxes correspond to the squares in the upper panel. The protein is shown in cartoon representation with the loops coloured as follows: T8, blue; L2, yellow; L3, black; L6, green. The citrate molecule is shown in space-filling representation. Citrate passes through the E-gate at ∼250 ns. Following citrate exit, the L2 loop moves back towards its initial conformation (black square), closing the pore once again. |
![[Figure 4]](be5250fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
