Fig. 2: The Pmt4–Ccw5 peptide binary complex. | Nature Communications

Fig. 2: The Pmt4–Ccw5 peptide binary complex.

From: Pmt4 recognizes two separate acceptor sites to O-mannosylate in the S/T-rich regions of substrate proteins

Fig. 2

Cryo-EM map processed by EMReady in a side (a) and top view (b). The MIR domains are removed in the top view to show the peptide density in the TMD groove. Pmt4-A is in cyan, and Pmt4-B is in teal. c A lipid and a dolichol bind in the transmembrane domain (TMD). d The MIR domains rotate and shift to bind the Ccw5 peptide. e Pmt4-B MIR motif loops 1–2 bind the Ccw5 peptide. f Ccw5 peptide in the peptide-binding groove of Pmt4-A. g Sequence alignment of S. cerevisiae Pmt1−7 in the peptide-binding groove. The six conserved groove residues are highlighted and combined into three doublets for double mutations: H83/H563, F313/N759, and L559/F662. h Phosphate release activity was assessed by incubating the Ccw5 peptide with purified WT or mutant Pmt4 proteins in the presence of Man-P. Control assays were performed with the peptide alone and the Pmt4 alone. Mean ± SD of three independent experiments, with all data points displayed as solid circles. Source data are provided as a Source Data file.

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