Comparison of the primary structure of PfPP5 with representative orthologs. The predicted sequences of PP5 from the following organisms (abbreviation and accession numbers in parenthesis) were aligned using the CLUSTALW multiple alignment program at the European Bioinformatics Institute (EMBL) server, and later refined by visual inspection: Plasmodium falciparum (Pf; AL049185); Trypanosoma brucei (Tb, AAG40278); S. cerevisiae (Sc, P53043); C. elegans (Ce, CAB60937); Drosophila melanogaster (Dm, AAF54438); Xenopus laevis (XI, AAB70574); Homo sapiens (Hs, AAD22669). The numbers of amino acid residues are shown on the right. The four proposed TPR domains of PfPP5, the spacer, and a helix are so indicated. Specific amino acid residues important in autoinhibition and interaction with hsp90 with mammalian PP5 are underlined on the bottom (human) sequence. Residues that are identical or conservative replacements (T, S; A, M, L, I, V; D, E; R, K; Q, N; F, Y) in at least 4 sequences are highlighted in gray. The TPR-deletion mutant starts at Met-273 (bold).