Fig. 5: Cryo-EM structure of the ternary Pmt4–Ccw5–Man complex. | Nature Communications

Fig. 5: Cryo-EM structure of the ternary Pmt4–Ccw5–Man complex.

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

Fig. 5

a Atomic model and density map around the catalytic pocket showing covalently linked Man to T122. b Surface charge view of the substrate-binding groove and catalytic pocket in Pmt4. c Structure of the Pmt4–Ccw5–Man with computationally docked Dol-P. The two right panels show H563 and H83 lining the substrate-binding groove near the acceptor T122 (upper) and five residues in the donor binding pocket coordinating the phosphate of the docked Dol-P (lower). d Proposed catalytic mechanism. See text for details.

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