Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii
Fig 6
HHPred identification of novel FO subunit a based on conserved structural features.
(A) Representation of the pairwise sequence alignments generated by HHPred [46,47] for the putative FO subunit a from T. gondii and 4 other FO subunit a proteins for which the structure is known. The table provides details of the amino acid length and a probability score for the prediction from the hit alignments. The red lines indicated the 3 transmembrane domains present in the T. gondii protein. (B) Protein sequence alignments and secondary structure information were made using the Clustal Omega [48] and ESPript [49] software, and only the C-terminal portion of respective proteins is shown. The names of alveolate species are highlighted in blue. For the nonalveolate species included in the alignment, the FO subunit a is either readily identified from sequence (Scer, Hsap, Atha, Ecol, and Pten) or has been experimentally determined (Crei and Poly). Positions with similar amino acids are highlighted in red in the alignment. The arginine and glutamine residues, highlighted in yellow, are conserved in all species and important for function. The helices (α9, α10, and α12) shown are from the structure of Poly F-type ATP synthase. Species names: Tgon, T. gondii; Hham, Hammondia hammondi; Pfal, P. falciparum; Pviv, P. vivax; Tann, Theileria annulata; Bbov, B. bovis; Cmur, C. muris; Cvel, C. velia; Crei, C. reinhardtii; Poly, Polytomella sp.; Scer, S. cerevisiae; Hsap, Homo sapiens; Atha, A. thaliana; Ecol, Escherichia coli; Pden, Paracoccus denitrificans.