Fig. 1. (A) Predicted tertiary structure of P. yoelii MyoA based on the crystal structure of chicken smooth muscle myosin. The ATP-binding pocket is shown with a bound ATP analog. The MyoA primary amino acid sequence corresponding to the neck domain is predicted to form an -helix. (B) Amino acid sequence alignment of P. yoelii (Py) MTIP, the MTIP ortholog from P. falciparum(Pf), obtained by BLAST analysis of the P. falciparum genome sequence information (Stanford_Chr12Contig01.010524, nucleotides 1931214-1031825) and the putative myosin light chain of T. gondii (Tg) (accession no. AY048862). The putative EF hand motif is indicated by asterisks. Identical amino acid residues are shown in white letters on black. Conserved amino acid changes are shown as white letters on gray. Radical amino acid changes are shown as black letters. The P. yoelii MTIP sequence is available from GenBank/EMBL/DDBJ under accession no. AF465245.