{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T01:46:29Z","timestamp":1792460789746,"version":"4.5.0"},"reference-count":33,"publisher":"National Academy of Sciences","issue":"13","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2007,3,27]]},"abstract":"<jats:p>\n                    Peptidoglycan is an essential polymer that forms a protective shell around bacterial cell membranes. Peptidoglycan biosynthesis is the target of many clinically used antibiotics, including the \u03b2-lactams, imipenems, cephalosporins, and glycopeptides. Resistance to these and other antibiotics has prompted interest in an atomic-level understanding of the enzymes that make peptidoglycan. Representative structures have been reported for most of the enzymes in the pathway. Until now, however, there have been no structures of any peptidoglycan glycosyltransferases (also known as transglycosylases), which catalyze formation of the carbohydrate chains of peptidoglycan from disaccharide subunits on the bacterial cell surface. We report here the 2.1-\u212b crystal structure of the peptidoglycan glycosyltransferase (PGT) domain of\n                    <jats:italic>Aquifex aeolicus<\/jats:italic>\n                    PBP1A. The structure has a different fold from all other glycosyltransferase structures reported to date, but it bears some resemblance to \u03bb-lysozyme, an enzyme that degrades the carbohydrate chains of peptidoglycan. An analysis of the structure, combined with biochemical information showing that these enzymes are processive, suggests a model for glycan chain polymerization.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0701160104","type":"journal-article","created":{"date-parts":[[2007,3,8]],"date-time":"2007-03-08T20:58:47Z","timestamp":1173387527000},"page":"5348-5353","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":150,"title":["Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis"],"prefix":"10.1073","volume":"104","author":[{"given":"Yanqiu","family":"Yuan","sequence":"first","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dianah","family":"Barrett","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yi","family":"Zhang","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Kahne","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Piotr","family":"Sliz","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry and Molecular Pharmacology and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suzanne","family":"Walker","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2007,3,27]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"publisher","DOI":"10.1039\/a804532a"},{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/9781555817886"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2006.07.066"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.2174\/187152606784112128"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0235749100"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6976.2006.00024.x"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1110\/ps.062112106"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.62.4.1079-1093.1998"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cbpa.2005.08.014"},{"key":"e_1_3_4_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.188.7.2528-2532.2006"},{"key":"e_1_3_4_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2006.03.012"},{"key":"e_1_3_4_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2005.10.030"},{"key":"e_1_3_4_13_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0407186102"},{"key":"e_1_3_4_14_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1997.1499"},{"key":"e_1_3_4_15_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi0028035"},{"key":"e_1_3_4_16_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1999.01612.x"},{"key":"e_1_3_4_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.184.13.3749-3752.2002"},{"key":"e_1_3_4_18_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M508646200"},{"key":"e_1_3_4_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.62.1.181-203.1998"},{"key":"e_1_3_4_20_2","doi-asserted-by":"publisher","DOI":"10.1099\/mic.0.26125-0"},{"key":"e_1_3_4_21_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0931492100"},{"key":"e_1_3_4_22_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi026205x"},{"key":"e_1_3_4_23_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja010028q"},{"key":"e_1_3_4_24_2","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/11.3.25R"},{"key":"e_1_3_4_25_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi051055m"},{"key":"e_1_3_4_26_2","author":"Zhang Y","year":"2007","unstructured":"Y Zhang, E Fechter, T-S Wang, D Barrett, S Walker, D Kahne J Am Chem Soc, 2007).","journal-title":"J Am Chem Soc"},{"key":"e_1_3_4_27_2","doi-asserted-by":"publisher","DOI":"10.1110\/ps.10301"},{"key":"e_1_3_4_28_2","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwj016"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","volume-title":"Macromolecular Crystallography, Part A","author":"Otwinowski Z","year":"1997","unstructured":"Z Otwinowski, W Minor, Methods in Enzymology. 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