view article
Figure 3
Comparison of MCR-2 with di-zinc MCR-1 and full-length EptA. (a) A close-up view of the MCR-2 di-zinc active site. Representations are as in Fig. 2[link]. Residues from symmetry-related molecules are coloured light red. (b) MCR-15LRM active site. (c) MCR-15GRR active site. (d) Superposition of the MCR-­2 catalytic domain with full-length EptA. The catalytic domains of MCR-2 (green) and EptA (cyan; PDB entry 5fgn; Anandan et al., 2017BB2) are superposed. The membrane domain of EptA is coloured grey; zinc ions are shown as grey spheres and bound DDM as purple sticks. Left: overall view with the N-terminus of MCR-2 labelled. Right: close-up of the active site with zinc-coordinating residues shown as sticks and the Zn2-coordinating water shown as a red sphere. MCR-2 Glu405 from a symmetry-related molecule is coloured pink.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 73| Part 8| August 2017| Pages 443-449
https://doi.org/10.1107/S2053230X17009669
Follow Acta Cryst. F
Sign up for e-alerts
E-alerts
Follow Acta Cryst. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS