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. 2012 Jul 18;7(7):e41083. doi: 10.1371/journal.pone.0041083

Figure 1. Anopheles gambiae mitochondrial carrier 1 (AgMC1) phylogeny and predicted structure.

Figure 1

(A) Phylogenetic tree based on the sequence alignment of the deduced amino acid sequence of AgMC1 (AGAP001297-PA) and the putative mitochondrial carriers from A. aegypti (AaMC1), D. melanogaster (DmMC1), human mitochondrial carriers HsSLC25A-39 and SLC25A-40 and yeast manganese trafficking factor for mitochondrial (ScMTM1); uncoupling proteins from humans (HsUCP), A. gambiae (AgUCP), A. aegypti (AaUCP) and D. melanogaster (DmUCP); putative adenine nucleotide translocators (ANT) from humans (HsANT, SLC25A6), yeast (ScANT), A. gambiae (AgANT) A. aegypti (AaANT), and D. melanogaster (DmANT); putative phosphate carriers (PiC) from humans (HsPiC, SLC25A3), yeast (ScPiC), A. gambiae (AgPiC), A. aegypti (AaPiC,) and D. melanogaster (DmPiC). Sequence alignments and accession numbers are included in Fig. S1. (B) Schematic representation of the AgMC1 protein sequence coding for three mitochondrial carrier domains (mito carr, top panel) highlighted in blue, green and red, and of the predicted secondary structure (bottom panel), consisting of six transmembrane domains (H1 to H6), three matrix domains, (M1 to M3), and cytosolic domains. (E) Predicted tertiary structure based on the amino acid sequence of the AgMC1 based on the known structure of bovine ADP/ATP adenine nucleotide translocator. Ribbon diagram of the predicted structure of AgMC1 from a lateral view (left), or viewed from either the matrix (top right) or intermembrane space side of the mitochondrial membrane (bottom right).