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Figure 3
Conformational changes associated with Met-AMP binding. (a) The structure of the active site of F-state MtMetRS (cyan) is superimposed with the active site of P-state MtMetRS (grey). The residues that make up the substrate-binding pockets are shown as stick models. The methionine pocket is highlighted in yellow and the AMP pocket is highlighted in blue. Met-AMP bound to the P-state enzyme is shown as a stick model (orange). Large structural rearrangements between these two structures are indicated by the dashed arrows with structural elements labelled in red. The inset shows the unusual β-turn conformation of the HVGH motif in F-state MtMetRS. Secondary-structure elements are labelled. (b) View from the opposite side to that in (a). Large rearrangements include the KMSKS loop, the α2 and α4 helices and the β3 strand.

IUCrJ
Volume 5| Part 4| July 2018| Pages 478-490
ISSN: 2052-2525
https://doi.org/10.1107/S2052252518008217