{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T11:55:41Z","timestamp":1789559741869,"version":"build-2803163510"},"reference-count":43,"publisher":"Portland Press Ltd.","issue":"7","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2017,4,1]]},"abstract":"<jats:p>Cysteine biosynthesis takes place via a two-step pathway in bacteria, fungi, plants and protozoan parasites, but not in humans, and hence, the machinery of cysteine biosynthesis is an opportune target for therapeutics. The decameric cysteine synthase complex (CSC) is formed when the C-terminal tail of serine acetyltransferase (SAT) binds in the active site of O-acetylserine sulfydrylase (OASS), playing a role in the regulation of this pathway. Here, we show that OASS from Brucella abortus (BaOASS) does not interact with its cognate SAT C-terminal tail. Crystal structures of native BaOASS showed that residues Gln96 and Tyr125 occupy the active-site pocket and interfere with the entry of the SAT C-terminal tail. The BaOASS (Q96A\u2013Y125A) mutant showed relatively strong binding (Kd\u2009=\u200932.4\u2005\u03bcM) to BaSAT C-terminal peptides in comparison with native BaOASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the SAT C-terminal end. Surface plasmon resonance results showed a relatively strong (7.3\u2005\u03bcM Kd) interaction between BaSAT and the BaOASS (Q96A\u2013Y125A), but no interaction with native BaOASS. Taken together, our observations suggest that the CSC does not form in B. abortus.<\/jats:p>","DOI":"10.1042\/bcj20161062","type":"journal-article","created":{"date-parts":[[2017,1,27]],"date-time":"2017-01-27T01:10:57Z","timestamp":1485479457000},"page":"1221-1239","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Structure-based mutational studies of <i>O<\/i>-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in <i>Brucella abortus<\/i>"],"prefix":"10.1042","volume":"474","author":[{"given":"Sudhaker","family":"Dharavath","sequence":"first","affiliation":[{"name":"School of Life Sciences, Jawaharlal Nehru University, New Delhi \u2013 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isha","family":"Raj","sequence":"additional","affiliation":[{"name":"School of Life Sciences, Jawaharlal Nehru University, New Delhi \u2013 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samudrala","family":"Gourinath","sequence":"additional","affiliation":[{"name":"School of Life Sciences, Jawaharlal Nehru University, New Delhi \u2013 110067, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2017,3,23]]},"reference":[{"key":"2021112216520617000_BCJ-2016-1062C1","doi-asserted-by":"publisher","first-page":"3767","DOI":"10.1002\/pmic.200500730","article-title":"Proteomic analysis of Brucella abortus cell envelope and identification of immunogenic candidate proteins for vaccine development","volume":"6","author":"Connolly","year":"2006","journal-title":"Proteomics"},{"key":"2021112216520617000_BCJ-2016-1062C2","doi-asserted-by":"publisher","first-page":"e1004853","DOI":"10.1371\/journal.ppat.1004853","article-title":"Brucella abortus induces the premature death of human neutrophils through the action of its lipopolysaccharide","volume":"11","author":"Barquero-Calvo","year":"2015","journal-title":"PLOS Pathog."},{"key":"2021112216520617000_BCJ-2016-1062C3","doi-asserted-by":"publisher","first-page":"e30305","DOI":"10.1371\/journal.pone.0030305","article-title":"Virtual screening, identification and in vitro testing of novel inhibitors of O-acetyl-l-serine sulfhydrylase of Entamoeba histolytica","volume":"7","author":"Nagpal","year":"2012","journal-title":"PLoS ONE"},{"key":"2021112216520617000_BCJ-2016-1062C4","doi-asserted-by":"publisher","first-page":"30629","DOI":"10.1074\/jbc.M111632200","article-title":"Use of biomolecular interaction analysis to elucidate the regulatory mechanism of the cysteine synthase complex from Arabidopsis thaliana","volume":"277","author":"Berkowitz","year":"2002","journal-title":"J. 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