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Efforts are underway to target the methionine biosynthesis pathway, as it is not part of the host metabolism. The homoserine transacetylase MetX converts\n                    <jats:sc>l<\/jats:sc>\n                    -homoserine to\n                    <jats:italic>O<\/jats:italic>\n                    -acetyl-\n                    <jats:sc>l<\/jats:sc>\n                    -homoserine at the committed step of this pathway. In order to facilitate structure-based drug design, we determined the high-resolution crystal structures of three MetX proteins, including\n                    <jats:italic>M. tuberculosis<\/jats:italic>\n                    (\n                    <jats:italic>Mt<\/jats:italic>\n                    MetX),\n                    <jats:italic>Mycolicibacterium abscessus<\/jats:italic>\n                    (\n                    <jats:italic>Ma<\/jats:italic>\n                    MetX), and\n                    <jats:italic>Mycolicibacterium hassiacum<\/jats:italic>\n                    (\n                    <jats:italic>Mh<\/jats:italic>\n                    MetX). A comparison of homoserine transacetylases from other bacterial and fungal species reveals a high degree of structural conservation amongst the enzymes. Utilizing homologous structures with bound cofactors, we analyzed the potential ligandability of MetX. The deep active-site tunnel surrounding the catalytic serine yielded many consensus clusters during mapping, suggesting that\n                    <jats:italic>Mt<\/jats:italic>\n                    MetX is highly druggable.\n                  <\/jats:p>","DOI":"10.1038\/s41598-019-56722-2","type":"journal-article","created":{"date-parts":[[2019,12,30]],"date-time":"2019-12-30T06:02:44Z","timestamp":1577685764000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site"],"prefix":"10.1038","volume":"9","author":[{"given":"Catherine T.","family":"Chaton","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emily S.","family":"Rodriguez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert W.","family":"Reed","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jian","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cameron W.","family":"Kenner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Konstantin V.","family":"Korotkov","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2019,12,30]]},"reference":[{"key":"56722_CR1","doi-asserted-by":"publisher","first-page":"a017798","DOI":"10.1101\/cshperspect.a017798","volume":"5","author":"P Glaziou","year":"2014","unstructured":"Glaziou, P., Sismanidis, C., Floyd, K. & Raviglione, M. 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