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Figure 5
Structural changes associated with activation. (a) Changes in the switch residues. Inactive VanRSc is shown in yellow and activated VanRSc is shown in slate blue. (b) Superposition of α4–β5–α5 in the inactive and activated states highlights the side-chain movements of polar interface residues, notably Arg111 and Arg118. (c) Stereoview of a mock dimer interface produced by superposing the inactive structure onto the activated structure. The resulting two inactive-state protomers are shown in green and yellow. Side-chain conformations in the inactive state are incompatible with the activated-state dimer interface: Arg111 and Tyr98 are too far apart to interact, as are Arg118 and Asp96. Additionally, the inactive-state conformation of Arg118 would clash with its symmetry mate.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 77| Part 8| August 2021| Pages 1027-1039
https://doi.org/10.1107/S2059798321006288
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