Extended Data Fig. 8: Sequence alignments of MPC subunits among different species.
From: Structures and mechanism of the human mitochondrial pyruvate carrier
a, Sequence alignment of MPC1. Sequences were obtained from UniProt with the following accession codes of MPC1 from corresponding species: Homo sapiens (Q9Y5U8), Mus musculus (P63030), Saccharomyces cerevisiae (P53157), Caenorhabditis elegans (Q21828), Drosophila melanogaster (Q7KSC4) and Danio rerio (F1Q6Z3). b, Sequence alignment of MPC2 from different species and MPC3 from S. cerevisiae. Sequences were obtained from UniProt with the following accession codes of MPC2 from corresponding species: H. sapiens (O95563), M. musculus (Q9D023), S. cerevisiae (P38857), C. elegans (O01578), D. melanogaster (Q9VHB2), D. rerio (Q7ZUJ3) and MPC3 from S. cerevisiae (P53311). In the sequence alignment results in a and b, residues forming the putative pyruvate-binding pocket in the occluded structure are indicated by reversed blue triangles, zipper-forming residues on L1 loops are indicated by reversed red triangles, residues mediating interactions between MPC1 and MPC2 below L1 loops are indicated by green squares, and UK5099-binding-pocket-forming residues are indicated by red dots. c, Difference in UK5099-binding pocket between human MPC and yeast MPC. Pockets were generated using PyMOL. The pocket of yeast MPC was mimicked by mutating corresponding residues in our UK5099-bound cryo-EM structure model. The opening of each binding pocket is highlighted by a red dashed line.
