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Interestingly, the bacterium <jats:italic>Bacillus anthracis<\/jats:italic> includes enzymes of the reverse transsulfuration pathway viz. cystathionine \u03b2\u2010synthase [Ba<jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content>, previously annotated to be an <jats:italic>O<\/jats:italic>\u2010acetylserine sulfhydrylase (<jats:styled-content style=\"fixed-case\">OASS<\/jats:styled-content>)] and cystathionine \u03b3\u2010lyase. Here, we report the structure of Ba<jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> at a resolution of 2.2 \u00c5. The enzyme was found to show <jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> activity only with activated serine (<jats:italic>O<\/jats:italic>\u2010acetylserine) and not with serine, and was also observed to display <jats:styled-content style=\"fixed-case\">OASS<\/jats:styled-content> activity but not serine sulfhydrylase activity. Ba<jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> was also found to produce hydrogen sulfide (H<jats:sub>2<\/jats:sub>S) upon reaction of cysteine and homocysteine. A mutational study revealed Glu 220, conserved in <jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content>, to be necessary for generating H<jats:sub>2<\/jats:sub>S. Structurally, Ba<jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> display a considerably more open active site than has been found for any other <jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> or <jats:styled-content style=\"fixed-case\">OASS<\/jats:styled-content>, which was attributed to the presence of a helix at the junction of the C\u2010 and N\u2010terminal domains. The root\u2010mean\u2010square deviation (<jats:styled-content style=\"fixed-case\">RMSD<\/jats:styled-content>) between the backbone C\u03b1 carbon atoms of Ba<jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> and those of other <jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content>s and <jats:styled-content style=\"fixed-case\">OASS<\/jats:styled-content>s were calculated to be greater than 3.0 \u00c5. The pyridoxal 5\u2032\u2010phosphate at the active site was not traced, and appeared to be highly flexible due to the active site being wide open. Phylogenetic analysis revealed the presence of an <jats:italic>O<\/jats:italic>\u2010acetylserine\u2010dependent <jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> in the bacterial domain and making separate clade from <jats:styled-content style=\"fixed-case\">CBS<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">OASS<\/jats:styled-content> indicating its evolution for specific function.<\/jats:p><\/jats:sec><jats:sec><jats:title>Database<\/jats:title><jats:p>Structural data are available in the <jats:styled-content style=\"fixed-case\">PDB<\/jats:styled-content> under the accession number <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5XW3\">5XW3<\/jats:ext-link>.<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.14273","type":"journal-article","created":{"date-parts":[[2017,9,18]],"date-time":"2017-09-18T14:11:18Z","timestamp":1505743878000},"page":"3862-3880","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Structural characterization and functional analysis of cystathionine \u03b2\u2010synthase: an enzyme involved in the reverse transsulfuration pathway of <i>Bacillus anthracis<\/i>"],"prefix":"10.1111","volume":"284","author":[{"given":"Suneeta","family":"Devi","sequence":"first","affiliation":[{"name":"Structural Biology Laboratory School of Life Sciences Jawaharlal Nehru University New Delhi India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Syed A.","family":"Abdul Rehman","sequence":"additional","affiliation":[{"name":"Structural Biology 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