{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T16:57:03Z","timestamp":1785430623084,"version":"3.56.0"},"reference-count":25,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2014,3,12]],"date-time":"2014-03-12T00:00:00Z","timestamp":1394582400000},"content-version":"vor","delay-in-days":70,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/3.0\/"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"crossref","award":["2011-4186"],"award-info":[{"award-number":["2011-4186"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100007676","name":"Ume\u00e5 Centre for Microbial Research","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100007676","id-type":"DOI","asserted-by":"crossref"}]},{"name":"National Research School in Odontology"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Open Bio"],"published-print":{"date-parts":[[2014,1]]},"abstract":"<jats:p>The pathogenic bacteria <jats:italic>Streptococcus pyogenes<\/jats:italic> can cause an array of diseases in humans, including moderate infections such as pharyngitis (strep throat) as well as life threatening conditions such as necrotizing fasciitis and puerperal fever. The antigen I\/II family proteins are cell wall anchored adhesin proteins found on the surfaces of most oral streptococci and are involved in host colonization and biofilm formation. In the present study we have determined the crystal structure of the C<jats:sub>2\u20133<\/jats:sub>\u2010domain of the antigen I\/II type protein AspA from <jats:italic>S. pyogenes<\/jats:italic> M type 28. The structure was solved to 1.8 \u00c5 resolution and shows that the C<jats:sub>2\u20133<\/jats:sub>\u2010domain is comprised of two structurally similar DEv\u2010IgG motifs, designated C<jats:sub>2<\/jats:sub> and C<jats:sub>3<\/jats:sub>, both containing a stabilizing covalent isopeptide bond. Furthermore a metal binding site is identified, containing a bound calcium ion. Despite relatively low sequence identity, interestingly, the overall structure shares high similarity to the C<jats:sub>2\u20133<\/jats:sub>\u2010domains of antigen I\/II proteins from <jats:italic>Streptococcus gordonii<\/jats:italic> and <jats:italic>Streptococcus mutans<\/jats:italic>, although certain parts of the structure exhibit distinct features. In summary this work constitutes the first step in the full structure determination of the AspA protein from <jats:italic>S. pyogenes<\/jats:italic>.\n<\/jats:p>","DOI":"10.1016\/j.fob.2014.02.012","type":"journal-article","created":{"date-parts":[[2014,3,14]],"date-time":"2014-03-14T15:16:19Z","timestamp":1394810179000},"page":"283-289","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Structure of the C\u2010terminal domain of AspA (antigen I\/II\u2010family) protein from <i>Streptococcus pyogenes<\/i>"],"prefix":"10.1002","volume":"4","author":[{"given":"Michael","family":"Hall","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c5sa","family":"Nylander","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Howard F.","family":"Jenkinson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karina","family":"Persson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2014,3,12]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0004166"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00772-08"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2007.05704.x"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2010.07212.x"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2010.01.065"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0912293107"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1107\/S174430911004443X"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111.231100"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(02)00025-6"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2011.07749.x"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444907050172"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1107\/S090744490705024X"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444904019158"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444912001308"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkq399"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444904023716"},{"key":"e_1_2_7_18_1","unstructured":"L.L.C. 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