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. 2023 Nov 13;42(24):e114889. doi: 10.15252/embj.2023114889

Figure 3. The acyl chain binding tunnel.

Figure 3

  • A
    C26‐CoA is coordinated by the TLC domain of Lac1 and the TM of Lip1.
  • B
    A hydrophobic tunnel for C26‐CoA acyl‐chain binding in Lac1.
  • C
    A close‐up view of the interactions between C26‐CoA acyl‐chain and the Lac1‐Lip1 complex. The residues lining the acyl chain binding tunnel are shown in sticks.
  • D
    Acyl‐chain selectivity of the Lac1‐Lip1 complex revealed by CerS activity. Each data point is the average ± SEM of three independent experiments.
  • E
    The distal end of the hydrophobic tunnel for C26‐CoA acyl‐chain coordination is not conserved. Lac1 is colored by the same amino acid conservation scores as in Fig 2C.
  • F, G
    Functional characterization of Lac1 (F) and Lip1 (G) hydrophobic residues for C26‐CoA acyl‐chain binding by CerS activity. Each data point is the average ± SEM of three independent experiments.

Source data are available online for this figure.