Mitochondrial Pyruvate Carrier 1 and 2 Heterodimer, In Silico, Models of Plant and Human Complexes: A Comparison of Structure and Transporter Binding Properties

The plant and human mitochondrial pyruvate carrier (MPC) had been studied in the 1970s-1990s providing many predictions on functional protein structure and mechanisms of substrate binding. Genes for human and plant MPC have been identified, but no crystal structure has yet been registered or deposited in a protein data bank. This report describes results for comparisons of structure for human and plant MPC1/2 heterodimer homology models. Key cysteine residues are identified for pyruvate and blocker binding and formation of thiohemiacetal or Michael addition bonds. Evidence is provided for an alternating access model in human, mouse ear-cress, castor and common beans, and corn.