{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T04:41:35Z","timestamp":1791434495046,"version":"4.3.3"},"reference-count":80,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2006,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Enterobacterial common antigen (ECA) is a polysaccharide found on the outer membrane of virtually all gram-negative enteric bacteria and consists of three sugars,\n            <jats:italic>N<\/jats:italic>\n            -acetyl-\n            <jats:sc>d<\/jats:sc>\n            -glucosamine,\n            <jats:italic>N<\/jats:italic>\n            -acetyl-\n            <jats:sc>d<\/jats:sc>\n            -mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-\n            <jats:sc>d<\/jats:sc>\n            -galactose, organized into trisaccharide repeating units having the sequence \u21923)-\u03b1-\n            <jats:sc>d<\/jats:sc>\n            -Fuc4NAc-(1\u21924)-\u03b2-\n            <jats:sc>d<\/jats:sc>\n            -ManNAcA-(1\u21924)-\u03b1-\n            <jats:sc>d<\/jats:sc>\n            -GlcNAc-(1\u2192. While the precise function of ECA is unknown, it has been linked to the resistance of Shiga-toxin-producing\n            <jats:italic>Escherichia coli<\/jats:italic>\n            (STEC) O157:H7 to organic acids and the resistance of\n            <jats:italic>Salmonella enterica<\/jats:italic>\n            to bile salts. The final step in the synthesis of 4-acetamido-4,6-dideoxy-\n            <jats:sc>d<\/jats:sc>\n            -galactose, the acetyl-coenzyme A (CoA)-dependent acetylation of the 4-amino group, is carried out by TDP-fucosamine acetyltransferase (WecD). We have determined the crystal structure of WecD in apo form at a 1.95-A\u030a resolution and bound to acetyl-CoA at a 1.66-A\u030a resolution. WecD is a dimeric enzyme, with each monomer adopting the GNAT\n            <jats:italic>N<\/jats:italic>\n            -acetyltransferase fold, common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars. The crystal structure of WecD, however, represents the first structure of a GNAT family member that acts on nucleotide sugars. Based on this cocrystal structure, we have used flexible docking to generate a WecD-bound model of the acetyl-CoA-TDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. Our structural data show that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of coenzyme A.\n          <\/jats:p>","DOI":"10.1128\/jb.00306-06","type":"journal-article","created":{"date-parts":[[2006,7,19]],"date-time":"2006-07-19T22:43:47Z","timestamp":1153349027000},"page":"5606-5617","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":26,"title":["Crystal Structure of TDP-Fucosamine Acetyltransferase (WecD) from\n            <i>Escherichia coli<\/i>\n            , an Enzyme Required for Enterobacterial Common Antigen Synthesis"],"prefix":"10.1128","volume":"188","author":[{"given":"Ming-Ni","family":"Hung","sequence":"first","affiliation":[{"name":"Biotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erumbi","family":"Rangarajan","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, McGill University, Montreal, Quebec Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Munger","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, McGill University, Montreal, Quebec Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guy","family":"Nadeau","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, McGill University, Montreal, Quebec Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Traian","family":"Sulea","sequence":"additional","affiliation":[{"name":"Biotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Allan","family":"Matte","sequence":"additional","affiliation":[{"name":"Biotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"2211","DOI":"10.1074\/jbc.M310134200","volume":"279","year":"2004","unstructured":"Allard, S. 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