page_title: Mitochondrial dicarboxylate carrier
section_title: Structure
hierarchical_section_title: Mitochondrial dicarboxylate carrier / Structure
caption_attribution_description: English: Crystal structure of a bacterial dicarboxylate carrier
context_page_description: The mitochondrial dicarboxylate carrier is an integral membrane protein encoded by the SLC25A10 gene in humans that catalyzes the transport of dicarboxylates such as malonate, malate, and succinate across the inner mitochondrial membrane in exchange for phosphate, sulfate, and thiosulfate by a simultaneous antiport mechanism, thus supplying substrates for the Krebs cycle, gluconeogenesis, urea synthesis, fatty acid synthesis, and sulfur metabolism.
context_section_description: The SLC25A10 gene is located on the q arm of chromosome 17 in position 25.3 and spans 8,781 base pairs. The gene has 11 exons and produces a 31.3 kDa protein composed of 287 amino acids. Intron 1 of this gene has five short Alu sequences. Mitochondrial dicarboxylate carriers are dimers, each consisting of six transmembrane domains with both the N- and C- terminus exposed to the cytoplasm. Like all mitochondrial carriers, dicarboxylate carriers features a tripartite structure with three repeats of about 100 amino acid residues, each of which contains a conserved sequence motif. These three tandem sequences fold into two anti-parallel transmembrane α-helices linked by hydrophilic sequences.
caption: Crystal structure of a bacterial dicarboxylate carrier
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