{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,27]],"date-time":"2026-05-27T21:14:07Z","timestamp":1779916447264,"version":"3.53.1"},"reference-count":35,"publisher":"International Union of Crystallography (IUCr)","issue":"9","license":[{"start":{"date-parts":[[2025,8,18]],"date-time":"2025-08-18T00:00:00Z","timestamp":1755475200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2025,8,18]],"date-time":"2025-08-18T00:00:00Z","timestamp":1755475200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"funder":[{"DOI":"10.13039\/501100017210","name":"Centre National de la Recherche Scientifique, Institut des Sciences Biologiques","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100017210","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"accepted":{"date-parts":[[2025,7,25]]},"published-print":{"date-parts":[[2025,9,1]]},"abstract":"<jats:p>Virulence protein J (VirJ) is a periplasmic protein encoded by the bacterial pathogen <jats:italic>Brucella abortus<\/jats:italic> and is important for its virulence. The VirJ homologue AcvB from <jats:italic>Agrobacterium tumefaciens<\/jats:italic> was found to be a lysyl-phosphatidylglycerol hydrolase that contains two domains, D1 and D2. Interestingly, both VirJ and AcvB are associated with the type IV secretion system (T4SS) activity in the respective bacteria. To date, no structural information is available for these proteins, limiting our understanding of their function. Here, we have purified, crystallized and determined the crystal structure of the N-terminal domain 1 of VirJ (VirJ<jats:sup>D1<\/jats:sup>) at a resolution of 1.7\u2005\u00c5. Our structural analysis shows that VirJ<jats:sup>D1<\/jats:sup> adopts an \u03b1\/\u03b2-hydrolase fold but lacks the characteristic catalytic triad. The structure presented here may help to decipher the function of VirJ in <jats:italic>Brucella<\/jats:italic> spp. and other bacterial pathogens, as well as its contribution to the T4SS function.<\/jats:p>","DOI":"10.1107\/s2053230x25006697","type":"journal-article","created":{"date-parts":[[2025,8,5]],"date-time":"2025-08-05T08:47:28Z","timestamp":1754383648000},"page":"374-380","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":5,"title":["Crystal structure of the virulence protein J (VirJ) domain 1 from <i>Brucella abortus<\/i>"],"prefix":"10.1107","volume":"81","author":[{"ORCID":"https:\/\/orcid.org\/0009-0009-6638-8400","authenticated-orcid":true,"given":"Chlo\u00e9","family":"Dugelay","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0007-0190-1934","authenticated-orcid":true,"given":"Sibylle","family":"Ferrarin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4279-9167","authenticated-orcid":true,"given":"Laurent","family":"Terradot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2025,8,18]]},"reference":[{"key":"ow5040_bb1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Cryst. 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