{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:52:20Z","timestamp":1786978340849,"version":"build-2736575974"},"reference-count":71,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2020,10,5]],"date-time":"2020-10-05T00:00:00Z","timestamp":1601856000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2020,11]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    PfSERA5, a significantly abundant protein present within the parasitophorous vacuole (PV) and essential for normal growth during the blood\u2010stage life cycle of the malaria parasite\n                    <jats:italic>Plasmodium falciparum<\/jats:italic>\n                    , displays structural similarity to many other cysteine proteases. However, PfSERA5 does not exhibit any detectable protease activity and therefore the role of the PfSERA5 papain\u2010like domain (PfSERA5E), thought to remain bound to its cognate prodomain, remains unknown. In this study, we present a revised structure of the central PfSERA5E domain at a resolution of 1.2 \u00c5, and the first structure of the \u201czymogen\u201d of this papain\u2010like domain including its cognate prodomain (PfSERA5PE) to 2.2 \u00c5 resolution. PfSERA5PE is somewhat structurally similar to that of other known proenzymes, retaining the conserved overall folding and orientation of the prodomain through, and occluding, the archetypal papain\u2010like catalytic triad \u201cactive\u2010site\u201d cleft, in the same reverse direction as conventional prodomains. Our findings are congruent with previously identified structures of PfSERA5E and of similar \u201czymogens\u201d and provide a foundation for further investigation into the function of PfSERA5.\n                  <\/jats:p>","DOI":"10.1002\/pro.3956","type":"journal-article","created":{"date-parts":[[2020,9,21]],"date-time":"2020-09-21T15:16:10Z","timestamp":1600701370000},"page":"2245-2258","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Structure of the\n                    <scp>\n                      <i>Plasmodium falciparum<\/i>\n                      PfSERA5\n                    <\/scp>\n                    pseudo\u2010zymogen"],"prefix":"10.1002","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8894-4249","authenticated-orcid":false,"given":"Nicholas A.","family":"Smith","sequence":"first","affiliation":[{"name":"Department of Chemistry and Physics, La Trobe Institute for Molecular Science La Trobe University  Melbourne Victoria Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1876-196X","authenticated-orcid":false,"given":"Oliver B.","family":"Clarke","sequence":"additional","affiliation":[{"name":"Department of Anesthesiology Columbia University  New York New York USA"},{"name":"Department of Physiology and Molecular Biophysics Columbia University  New York New York USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3006-2483","authenticated-orcid":false,"given":"Mihwa","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science La Trobe University  Melbourne Victoria Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony N.","family":"Hodder","sequence":"additional","affiliation":[{"name":"The Walter and Eliza Hall Institute of Medical Research  Melbourne Victoria Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0498-1910","authenticated-orcid":false,"given":"Brian J.","family":"Smith","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Physics, La Trobe Institute for Molecular Science La Trobe University  Melbourne Victoria Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2020,10,5]]},"reference":[{"key":"e_1_2_16_2_1","unstructured":"World Health Organization. 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