Fig. 1: Identification of the Na-pump binding site on zDHHC5. | Communications Biology

Fig. 1: Identification of the Na-pump binding site on zDHHC5.

From: Control of protein palmitoylation by regulating substrate recruitment to a zDHHC-protein acyltransferase

Fig. 1

a The Na-pump was purified from rat ventricular lysate using an array of overlapping peptides covering zDHHC5 region αα 218–334. A binding peak comprising three overlapping peptides centered on peptide αα 233–257, the Na-pump binding site peptide (NBSP), was observed. b Alignment of the zDHHC5 and 20 C-terminal domains in the region of their TTxE and PaACT motifs. c The PaACT motifs of both zDHHC5 and 20 contain an amphipathic helix (red, non-polar; purple, polar). d Structural model of the NBSP based on the structure of zDHHC20 (PDB accession code 6BML) with putative sites of post-translational modification shown (palmitoylation, yellow; GlcNAcylation, green). e The position of the NBSP (blue) on the structure of zDHHC20 (PDB 6BML). The NBSP is located a considerable distance from the enzyme active site (C of zDHHC motif, pink; 2-bromopalmitate, red) suggesting that the interaction between zDHHC5 and PLM is likely to be indirect. Figure 1d, e were made using MacPYMOL.

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