{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,12]],"date-time":"2026-04-12T08:34:02Z","timestamp":1775982842487,"version":"3.50.1"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009797","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,8,16]],"date-time":"2021-08-16T00:00:00Z","timestamp":1629072000000}}],"reference-count":77,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T00:00:00Z","timestamp":1627516800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"australian government research training program scholarship"},{"name":"australian government research training program scholarship"},{"name":"australian government research training program scholarship"},{"name":"nhmrc overseas biomedical fellowship","award":["1016357"],"award-info":[{"award-number":["1016357"]}]},{"DOI":"10.13039\/501100000925","name":"national health and medical research council","doi-asserted-by":"publisher","award":["APP1129843"],"award-info":[{"award-number":["APP1129843"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000923","name":"australian research council","doi-asserted-by":"crossref","award":["DP150102883"],"award-info":[{"award-number":["DP150102883"]}],"id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Coenzyme A is synthesised from pantothenate via five enzyme-mediated steps. The first step is catalysed by pantothenate kinase (PanK). All PanKs characterised to date form homodimers. Many organisms express multiple PanKs. In some cases, these PanKs are not functionally redundant, and some appear to be non-functional. Here, we investigate the PanKs in two pathogenic apicomplexan parasites,\n                    <jats:italic>Plasmodium falciparum<\/jats:italic>\n                    and\n                    <jats:italic>Toxoplasma gondii<\/jats:italic>\n                    . Each of these organisms express two PanK homologues (PanK1 and PanK2). We demonstrate that\n                    <jats:italic>Pf<\/jats:italic>\n                    PanK1 and\n                    <jats:italic>Pf<\/jats:italic>\n                    PanK2 associate, forming a single, functional PanK complex that includes the multi-functional protein,\n                    <jats:italic>Pf<\/jats:italic>\n                    14-3-3I. Similarly, we demonstrate that\n                    <jats:italic>Tg<\/jats:italic>\n                    PanK1 and\n                    <jats:italic>Tg<\/jats:italic>\n                    PanK2 form a single complex that possesses PanK activity. Both\n                    <jats:italic>Tg<\/jats:italic>\n                    PanK1 and\n                    <jats:italic>Tg<\/jats:italic>\n                    PanK2 are essential for\n                    <jats:italic>T<\/jats:italic>\n                    .\n                    <jats:italic>gondii<\/jats:italic>\n                    proliferation, specifically due to their PanK activity. Our study constitutes the first examples of heteromeric PanK complexes in nature and provides an explanation for the presence of multiple PanKs within certain organisms.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1009797","type":"journal-article","created":{"date-parts":[[2021,7,29]],"date-time":"2021-07-29T14:48:33Z","timestamp":1627570113000},"page":"e1009797","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":18,"title":["A novel heteromeric pantothenate kinase complex in apicomplexan parasites"],"prefix":"10.1371","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1711-0815","authenticated-orcid":true,"given":"Erick T.","family":"Tjhin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9052-2037","authenticated-orcid":true,"given":"Vanessa M.","family":"Howieson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8156-7070","authenticated-orcid":true,"given":"Christina","family":"Spry","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2455-9821","authenticated-orcid":true,"given":"Giel G.","family":"van Dooren","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3345-8440","authenticated-orcid":true,"given":"Kevin J.","family":"Saliba","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2021,7,29]]},"reference":[{"key":"ppat.1009797.ref001","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.plipres.2005.04.001","article-title":"Coenzyme A: back in action","volume":"44","author":"R Leonardi","year":"2005","journal-title":"Prog Lipid Res"},{"key":"ppat.1009797.ref002","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1111\/j.1574-6976.2007.00093.x","article-title":"Coenzyme A biosynthesis: an antimicrobial drug target","volume":"32","author":"C Spry","year":"2008","journal-title":"FEMS Microbiol Rev"},{"key":"ppat.1009797.ref003","doi-asserted-by":"crossref","first-page":"28093","DOI":"10.1074\/jbc.M003190200","article-title":"Structural basis for the feedback regulation of Escherichia coli pantothenate kinase by coenzyme A","volume":"275","author":"M Yun","year":"2000","journal-title":"J Biol Chem"},{"key":"ppat.1009797.ref004","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1107\/S0907444906012728","article-title":"Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanK","volume":"62","author":"S Das","year":"2006","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"ppat.1009797.ref005","doi-asserted-by":"crossref","first-page":"5532","DOI":"10.1128\/JB.00469-06","article-title":"Crystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria","volume":"188","author":"K Yang","year":"2006","journal-title":"J Bacteriol"},{"key":"ppat.1009797.ref006","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1016\/j.str.2006.06.008","article-title":"Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties","volume":"14","author":"BS Hong","year":"2006","journal-title":"Structure"},{"key":"ppat.1009797.ref007","doi-asserted-by":"crossref","first-page":"3234","DOI":"10.1021\/bi062299p","article-title":"Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 \u00c5 resolution: implications for coenzyme A-dependent redox biology","volume":"46","author":"NI Nicely","year":"2007","journal-title":"Biochemistry"},{"key":"ppat.1009797.ref008","first-page":"27984","article-title":"Crystal structures of human pantothenate kinases. 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