{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:04:02Z","timestamp":1787011442590,"version":"build-2736575974"},"reference-count":46,"publisher":"International Union of Crystallography (IUCr)","issue":"12","license":[{"start":{"date-parts":[[2019,11,29]],"date-time":"2019-11-29T00:00:00Z","timestamp":1574985600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2019,11,29]],"date-time":"2019-11-29T00:00:00Z","timestamp":1574985600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institutes of Health, National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["2R01AI057393"],"award-info":[{"award-number":["2R01AI057393"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Struct Biol","Acta Crystallogr D","Acta Cryst D","Acta Cryst D Struct Biol","Acta Cryst Sect D","Acta Cryst Sect D Struct Biol","Acta Crystallogr Sect D","Acta Crystallogr Sect D Struct Biol","Acta Crystallogr D Biol Crystallogr","Acta Cryst D Biol Cryst"],"accepted":{"date-parts":[[2019,11,7]]},"published-print":{"date-parts":[[2019,12,1]]},"abstract":"<jats:p>\n                    Aminoglycoside phosphotransferases (APHs) are one of three families of aminoglycoside-modifying enzymes that confer high-level resistance to the aminoglycoside antibiotics via enzymatic modification. This has now rendered many clinically important drugs almost obsolete. The APHs specifically phosphorylate hydroxyl groups on the aminoglycosides using a nucleotide triphosphate as the phosphate donor. The APH(2\u2032\u2032) family comprises four distinct members, isolated primarily from\n                    <jats:italic>Enterococcus<\/jats:italic>\n                    sp., which vary in their substrate specificities and also in their preference for the phosphate donor (ATP or GTP). The structure of the ternary complex of APH(2\u2032\u2032)-IIIa with GDP and kanamycin was solved at 1.34\u2005\u00c5 resolution and was compared with substrate-bound structures of APH(2\u2032\u2032)-Ia, APH(2\u2032\u2032)-IIa and APH(2\u2032\u2032)-IVa. In contrast to the case for APH(2\u2032\u2032)-Ia, where it was proposed that the enzyme-mediated hydrolysis of GTP is regulated by conformational changes in its N-terminal domain upon GTP binding, APH(2\u2032\u2032)-IIa, APH(2\u2032\u2032)-IIIa and APH(2\u2032\u2032)-IVa show no such regulatory mechanism, primarily owing to structural differences in the N-terminal domains of these enzymes.\n                  <\/jats:p>","DOI":"10.1107\/s2059798319015079","type":"journal-article","created":{"date-parts":[[2019,11,29]],"date-time":"2019-11-29T06:25:12Z","timestamp":1575008712000},"page":"1129-1137","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":7,"title":["Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside-2\u2032\u2032-phosphotransferases"],"prefix":"10.1107","volume":"75","author":[{"given":"Clyde A.","family":"Smith","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Toth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nichole K.","family":"Stewart","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lauren","family":"Maltz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergei B.","family":"Vakulenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2019,11,29]]},"reference":[{"key":"mn5123_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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