Fig. 5: Conformational changes of MPC in a pyruvate transport cycle.
From: Structure of human mitochondrial pyruvate carrier MPC1 and MPC2 complex
a Structural alignment of MPC1-2 complex in IMS-open and matrix-open states performed using PyMOL, shown as side and top views. The “rotation center” is indicated by a dashed parallelogram in the left panel and the residues located at the rotation center were shown as sticks in the right panel. b Electrostatic surface representations of MPC1-2 complex at IMS-open and matrix-open states. The residues located at the rotation center were shown as sticks. c Structural comparison of MPC1 and MPC2 at different states. The binding of TM1 at the Pro37 (red) in MPC1 is indicated by an arrow. The binding of TM1 at the Gly56 (red) in MPC2 is indicated by an arrow. d Serial dilutions of wild-type (WT), mpc2Δmpc3Δ and mpc1Δ yeast strains spotted on medium lacking leucine (-URA-LEU). The mpc1Δ cells were transformed with wild-type MPC1 or MPC1P37V. The mpc2Δmpc3Δ cells were co-transformed with wild-type MPC1 and wild-type MPC2 or MPC2G56A. e A working model for pyruvate transport by MPC. Created in BioRender. Qi, X. (2025) https://BioRender.com/todji9n.
