{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T12:19:14Z","timestamp":1790252354856,"version":"4.1.0"},"reference-count":30,"publisher":"National Academy of Sciences","issue":"8","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2006,2,21]]},"abstract":"<jats:p>\n                    Bacterial type IV secretion systems (T4SS) translocate DNA and\/or proteins to recipient cells, thus providing a mechanism for conjugative transfer of genetic material and bacterial pathogenesis. Here we describe the first structure of a core component from the archetypal\n                    <jats:italic>Agrobacterium tumefaciens<\/jats:italic>\n                    T4SS: the 2.2-\u00c5 resolution crystal structure of the VirB8 periplasmic domain (pVirB8\n                    <jats:sup>AT<\/jats:sup>\n                    ). VirB8 forms a dimer in the crystal, and we identify residues likely important for stabilization of the dimer interface. Structural comparison of pVirB8\n                    <jats:sup>AT<\/jats:sup>\n                    with\n                    <jats:italic>Brucella suis<\/jats:italic>\n                    VirB8 confirms that the monomers have a similar fold. In addition, the pVirB8\n                    <jats:sup>AT<\/jats:sup>\n                    dimer superimposes very closely on the\n                    <jats:italic>B. suis<\/jats:italic>\n                    VirB8 dimer, supporting the proposal that dimer formation in the crystal reflects self-interactions that are biologically significant. The evolutionary conservation level for each residue was obtained from a data set of 84 VirB8 homologs and projected onto the protein structure to indicate conserved surface patches that likely contact other T4SS proteins.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0511216103","type":"journal-article","created":{"date-parts":[[2006,2,15]],"date-time":"2006-02-15T20:44:32Z","timestamp":1140036272000},"page":"2582-2587","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":75,"title":["<i>Agrobacterium tumefaciens<\/i>\n                    VirB8 structure reveals potential protein\u2013protein interaction sites"],"prefix":"10.1073","volume":"103","author":[{"given":"Susan","family":"Bailey","sequence":"first","affiliation":[{"name":"*Molecular Biophysics Group, Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Warrington WA4 4AD, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Doyle","family":"Ward","sequence":"additional","affiliation":[{"name":"Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecca","family":"Middleton","sequence":"additional","affiliation":[{"name":"Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. Gunter","family":"Grossmann","sequence":"additional","affiliation":[{"name":"*Molecular Biophysics Group, Council for the Central Laboratory of the Research Councils Daresbury Laboratory, Warrington WA4 4AD, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia C.","family":"Zambryski","sequence":"additional","affiliation":[{"name":"Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2006,2,15]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev.micro.58.030603.123630","volume":"59","author":"Christie P. J.","year":"2005","unstructured":"P. J. Christie, K. Atmakuri, V. Krishnamoorthy, S. Jakubowski, E. Cascales Annu. Rev. Microbiol 59, 451\u2013485 (2005).","journal-title":"Annu. Rev. 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