{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,14]],"date-time":"2025-11-14T16:59:01Z","timestamp":1763139541307,"version":"3.45.0"},"reference-count":66,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2025,11,14]],"date-time":"2025-11-14T00:00:00Z","timestamp":1763078400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>Type-P5 ATPases are the least characterized among the P-type ATPases and this is especially true in the case of the malaria parasite. In this study, Spf1, a subtype-P5A ATPase of yeast, and ATP13A2, a subtype-P5B ATPase of humans, were used as templates to extensively characterize the sequences and structural features of haemosporidian type-P5 ATPases. Malaria parasites have both subtype-P5A and subtype-P5B ATPase genes and the structural features of the proteins recapitulate the known structures of subtype-P5A and subtype-P5B ATPases. Detailed structural analysis detected an additional \u03b1-helix in the P-domain of subtype-P5A ATPases, which is not found in subtype-P5B ATPases. This feature may be an additional signature to distinguish subtype-P5A and subtype-P5B ATPases, in addition to the previously described differences in the membrane loops of the N-terminal domain, the arm in the P-domain of subtype-P5A, and substrate differences. A notable difference in the type-P5 ATPases from the malaria parasite, as compared to the templates, is the insertion of multiple variable and low-complexity regions that form intrinsically disorganized loops. These loops may form a shroud-like structure that protects the core ATPase structure and\/or participates in low-affinity interprotein interactions. Homology modeling did not provide definitive answers about the substrate specificity of the haemosporidian type-P5 ATPases. However, the haemosporidian subtype-P5A ATPase is likely an ER transmembrane dislocase as are the other subtype-P5A ATPases. In contrast, the subtype-P5B ATPases of the malaria parasite are not likely to be polyamine transporters in lysosomes, as have been described in fungi and metazoans. This suggests that subtype-P5B ATPases have undergone lineage-specific divergence in regard to their function(s).<\/jats:p>","DOI":"10.3390\/pathogens14111164","type":"journal-article","created":{"date-parts":[[2025,11,14]],"date-time":"2025-11-14T16:46:22Z","timestamp":1763138782000},"page":"1164","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Homology Modeling of Type-P5 ATPases from the Malaria Parasite: Insight into Their Functions and Evolution, and Implications About the Effect and Role of Intrinsically Disordered Protein Structure"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5893-9983","authenticated-orcid":false,"given":"Mark F.","family":"Wiser","sequence":"first","affiliation":[{"name":"Department of Tropical Medicine and Infectious Disease, Celia Scott Weatherhead School of Public Health & Tropical Medicine, Tulane University, New Orleans, LA 70112, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2025,11,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Palmgren, M. 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