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These diseases remain a significant health problem both in endemic countries and globally. These parasites and other trypanosomatids, including\n                    <jats:italic>T. theileri<\/jats:italic>\n                    , a bovine pathogen, rely on cysteine biosynthesis for the production of trypanothione, which is essential for parasite survival in hosts. The\n                    <jats:italic>de novo<\/jats:italic>\n                    pathway of cysteine biosynthesis requires the conversion of\n                    <jats:italic>O<\/jats:italic>\n                    -acetyl-L-serine into L-cysteine, which is catalysed by cysteine synthase (CS). These enzymes present potential for drug development against\n                    <jats:italic>T.\u00a0cruzi<\/jats:italic>\n                    ,\n                    <jats:italic>Leishmania<\/jats:italic>\n                    spp. and\n                    <jats:italic>T. theileri<\/jats:italic>\n                    . To enable these possibilities, biochemical and crystallographic studies of CS from\n                    <jats:italic>T. cruzi<\/jats:italic>\n                    (\n                    <jats:italic>Tc<\/jats:italic>\n                    CS),\n                    <jats:italic>L.\u00a0infantum<\/jats:italic>\n                    (\n                    <jats:italic>Li<\/jats:italic>\n                    CS)  and\n                    <jats:italic>T.\u00a0theileri<\/jats:italic>\n                    (\n                    <jats:italic>Tth<\/jats:italic>\n                    CS) were conducted. Crystal structures of the three enzymes were determined at resolutions of 1.80\u2005\u00c5 for\n                    <jats:italic>Tc<\/jats:italic>\n                    CS, 1.75\u2005\u00c5 for\n                    <jats:italic>Li<\/jats:italic>\n                    CS and 2.75\u2005\u00c5 for\n                    <jats:italic>Tth<\/jats:italic>\n                    CS. These three homodimeric structures show the same overall fold and demonstrate that the active-site geometry is conserved, supporting a common reaction mechanism. Detailed structural analysis revealed reaction intermediates of the\n                    <jats:italic>de novo<\/jats:italic>\n                    pathway ranging from an apo structure of\n                    <jats:italic>Li<\/jats:italic>\n                    CS and holo structures of both\n                    <jats:italic>Tc<\/jats:italic>\n                    CS and\n                    <jats:italic>Tth<\/jats:italic>\n                    CS to the substrate-bound structure of\n                    <jats:italic>Tc<\/jats:italic>\n                    CS. These structures will allow exploration of the active site for the design of novel inhibitors. Additionally, unexpected binding sites discovered at the dimer interface represent new potential for the development of protein\u2013protein inhibitors.\n                  <\/jats:p>","DOI":"10.1107\/s2059798323003613","type":"journal-article","created":{"date-parts":[[2023,5,9]],"date-time":"2023-05-09T07:31:42Z","timestamp":1683617502000},"page":"518-530","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":7,"title":["Cysteine synthase: multiple structures of a key enzyme in cysteine synthesis and a potential drug target for Chagas disease and leishmaniasis"],"prefix":"10.1107","volume":"79","author":[{"given":"Kate","family":"Sowerby","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01v29qb04","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Chemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1423-8103","authenticated-orcid":true,"given":"Stefanie","family":"Freitag-Pohl","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01v29qb04","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Chemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Milena","family":"Murillo","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/036rp1748","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Parasitology"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ariel Mariano","family":"Silber","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/036rp1748","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Parasitology"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9949-4471","authenticated-orcid":true,"given":"Ehmke","family":"Pohl","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/01v29qb04","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Chemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2023,5,19]]},"reference":[{"key":"di5064_bb1","doi-asserted-by":"crossref","first-page":"e0004458","DOI":"10.1371\/journal.pntd.0004458","volume":"10","author":"Alten","year":"2016","journal-title":"PLoS Negl. 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