Extended Data Fig. 4: Conservation and metal ligand binding of myozoan Cox13.
From: Structure, assembly and inhibition of the Toxoplasma gondii respiratory chain supercomplex
(a) T. gondii CIV structure (b) TgApiCox13 with bound lipids (CDL, cardiolipin; PE, phosphatidylethanolamine) (c) ApiCox13 from T. gondii (left, this study), predicted homolog structures from Perkinsus marinus and Plasmodium falciparum. Of the two Fe2S2 clusters in T. gondii, one is conserved in P. falciparum, whereas P. marinus seem to utilize zinc. Insets show Fe2S2 coordination sites. (d) Phylogenetic tree with conservation of Fe2S2 and zinc (e) Multi-sequence alignment with residues involved in Fe2S2 or zinc binding shown in yellow and orange respectively. (f) Cofacors of the T. gondii respiratory supercomplex. The Zn2+ of the MPP-beta subunits and the Fe2S2 iron-sulfur clusters in TgApiCox13 that are not part of the electron transfer pathway are indicated with respective subunit names.
