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Figure 2
Structure of AoRib2. (a) The deaminase domain is made up of a central β-sheet flanked by α-­helices. The endogenous zinc ion in the deaminase domain is shown as a magenta sphere. (b) Sedimentation-velocity analysis of AoRib2. The enzyme concentration was 0.3 mg ml−1 in 20 mM PBS pH 7.5. The three panels represent the optical traces (top), the residuals of the model fitting (middle) and the sedimentation-coefficient distribution (bottom). The ultracentrifugation analysis demonstrated that AoRib2 exists as a monomer in solution. (c) Structural superposition of AoRib2 (red), yCD (green), BsRibG (blue) and EcTadA (yellow). They share a similar structural core (gray) but show divergence in the C-terminal helices.

IUCrJ
Volume 8| Part 4| July 2021| Pages 549-558
ISSN: 2052-2525
https://doi.org/10.1107/S205225252100275X