{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T02:06:37Z","timestamp":1771293997915,"version":"3.50.1"},"reference-count":56,"publisher":"International Union of Crystallography (IUCr)","issue":"11","license":[{"start":{"date-parts":[[2014,10,29]],"date-time":"2014-10-29T00:00:00Z","timestamp":1414540800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2014,10,29]],"date-time":"2014-10-29T00:00:00Z","timestamp":1414540800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Biol Crystallogr","Acta Crystallogr D","Acta Crystallogr D Biol Cryst","Acta Cryst D","Acta Cryst D Biol Crystallogr","Acta Cryst D Biol Cryst","Acta Cryst Sect D","Acta Cryst Sect D Biol Cryst","Acta Crystallogr Sect D","Acta Crystallogr Sect D Biol Crystallogr"],"published-print":{"date-parts":[[2014,11,1]]},"abstract":"<jats:p><jats:italic>Mycobacterium abscessus<\/jats:italic>is the most pathogenic rapid-growing mycobacterium and is one of the most resistant organisms to chemotherapeutic agents. However, structural and functional studies of<jats:italic>M. abscessus<\/jats:italic>proteins that could modify\/inactivate antibiotics remain nonexistent. Here, the structural and functional characterization of an arylamine<jats:italic>N<\/jats:italic>-acetyltransferase (NAT) from<jats:italic>M. abscessus<\/jats:italic>[(MYCAB)NAT1] are reported. This novel prokaryotic NAT displays significant<jats:italic>N<\/jats:italic>-acetyltransferase activity towards aromatic substrates, including antibiotics such as isoniazid and<jats:italic>p<\/jats:italic>-aminosalicylate. The enzyme is endogenously expressed and functional in both the rough and smooth<jats:italic>M. abscessus<\/jats:italic>morphotypes. The crystal structure of (MYCAB)NAT1 at 1.8\u2005\u00c5 resolution reveals that it is more closely related to<jats:italic>Nocardia farcinica<\/jats:italic>NAT than to mycobacterial isoforms. In particular, structural and physicochemical differences from other mycobacterial NATs were found in the active site. Peculiarities of (MYCAB)NAT1 were further supported by kinetic and docking studies showing that the enzyme was poorly inhibited by the piperidinol inhibitor of mycobacterial NATs. This study describes the first structure of an antibiotic-modifying enzyme from<jats:italic>M. abscessus<\/jats:italic>and provides bases to better understand the substrate\/inhibitor-binding specificities among mycobacterial NATs and to identify\/optimize specific inhibitors. These data should also contribute to the understanding of the mechanisms that are responsible for the pathogenicity and extensive chemotherapeutic resistance of<jats:italic>M. abscessus<\/jats:italic>.<\/jats:p>","DOI":"10.1107\/s1399004714021282","type":"journal-article","created":{"date-parts":[[2014,10,28]],"date-time":"2014-10-28T15:08:58Z","timestamp":1414508938000},"page":"3066-3079","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":12,"title":["Structural and functional characterization of an arylamine<i>N<\/i>-acetyltransferase from the pathogen<i>Mycobacterium abscessus<\/i>: differences from other mycobacterial isoforms and implications for selective inhibition"],"prefix":"10.1107","volume":"70","author":[{"given":"Ang\u00e9lique","family":"Cocaign","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xavier","family":"Kubiak","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ximing","family":"Xu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guillaume","family":"Garnier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"In\u00e8s","family":"Li de la Sierra-Gallay","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Linh","family":"Chi-Bui","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julien","family":"Dairou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Florent","family":"Busi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Areej","family":"Abuhammad","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ahmed","family":"Haouz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean-Marie","family":"Dupret","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean-Louis","family":"Herrmann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fernando","family":"Rodrigues-Lima","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"329","published-online":{"date-parts":[[2014,10,29]]},"reference":[{"key":"yt5074_bb1","doi-asserted-by":"crossref","first-page":"e52790","DOI":"10.1371\/journal.pone.0052790","volume":"7","author":"Abuhammad","year":"2012","journal-title":"PLoS One"},{"key":"yt5074_bb2","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1107\/S0907444913015126","volume":"69","author":"Abuhammad","year":"2013","journal-title":"Acta Cryst. 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