Supplementary Figure 3: Comparison of budding yeast Cdc14 with human Cdc14B.
From: A PxL motif promotes timely cell cycle substrate dephosphorylation by the Cdc14 phosphatase
(a), Overlay of human Cdc14B (PDB ID: 1OHE; blue) and an S. cerevisiae Cdc14 protomer (gray), bound by the Cbk1 peptide (pink), demonstrates their similar overall fold (root-mean-square deviation of 0.89 Å over 242 Cα atoms). (b), Structure of the Cdc14-Cbk1 peptide complex. Each Cdc14 protomer (shades of gray) binds a Cbk1 peptide (pink). Close-up views of the MES buffer molecule bound to an active site and a zinc binding site are shown. (c), Anomalous difference electron density map indicating a density peak corresponding to zinc. The electron density is contoured at 7σ. For details regarding data collection, see Table 1. The zinc binding sites of both Cdc14 protomers are shown.
