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Figure 4
A product complex of mature mirolysin. (a) Superposition of the Cα plots of promirolysin (PS in pink, CD in light blue) and mature mirolysin (purple) in the orientation of Fig. 2[link](a). Significantly deviating regions are pinpointed by green arrows. The catalytic zinc and the structural calcium cations are shown as magenta and blue spheres, respectively. (b) Detail of the initial Fourier omit map to 1.5 Å of the product complex around the citrate (CIT−1) and the tetradecapeptide (Lys1–Lys14), both as stick models with green carbons and labels. The map (in orange) is contoured at 0.6σ above threshold and is clear for CIT−1 and the main and side chains of Lys1–Ile8 and Ser11–Thr12, as well as for the main chains of Lys9, Leu10, Ile13 and Lys14. The view results from an ∼45° rotation downward from the standard orientation of Fig. 2[link](a). (c) Close-up view of mature mirolysin (carbons in plum) and the product (carbons in green) resulting from the view in (a) after a vertical 90° rotation to the left. Selected residues are labelled with their residue numbers in purple and dark green, respectively.

IUCrJ
Volume 7| Part 1| January 2020| Pages 18-29
ISSN: 2052-2525
https://doi.org/10.1107/S2052252519013848