Figure 5
Loop 3 provides necessary flexibility in the ABS of bacterial GUSs. (a) The B-factor putty image of the TIM barrel domain of the RgGUS/UIFG complex and the molecular structure of UIFG. The relatively large B-factor of loop 3 in RgGUS indicates a large degree of flexibility. (b) The RMSFs of the Cα atoms of apo CpGUS and the CpGUS/10 complex are shown for 20-ns MD simulations. (c) The differences in the RMSFs were calculated the Cα atoms in apo CpGUS and the CpGUS/10 complex. Loop 3 is the most mobile loop in apo CpGUS and the CpGUS/10 complex. The RMSF difference of the two forms of CpGUS suggests that the flexibility of loop 3 decreased upon substrate binding. Although the Cα atoms of CpGUS loop 5 seem mobile, side-chain movements of loop 5 residues were observed during the MD simulations.
