{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,9]],"date-time":"2026-06-09T12:00:14Z","timestamp":1781006414145,"version":"3.54.1"},"reference-count":26,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2024,9,9]],"date-time":"2024-09-09T00:00:00Z","timestamp":1725840000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2025,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Aminoglycoside antibiotics have played a critical role in the treatment of both Gram\u2010negative and Gram\u2010positive bacterial infections. However, antibiotic resistance has severely compromised the efficacy of aminoglycosides. A leading cause of aminoglycoside resistance is mediated by bacterial enzymes that inactivate these drugs via chemical modification. Aminoglycoside nucleotidyltransferase\u20106 (ANT(6)) enzymes inactivate streptomycin by transferring an adenyl group from ATP to position 6 on the antibiotic. Despite the clinical significance of this activity, ANT(6) enzymes remain relatively uncharacterized. Here, we report the first high resolution x\u2010ray crystallographic structure of ANT(6)\u2010Ib from\n                    <jats:italic>Campylobacter fetus<\/jats:italic>\n                    subsp.\n                    <jats:italic>fetus<\/jats:italic>\n                    bound with streptomycin. Structural modeling and gel filtration chromatography experiments suggest that the enzyme exists as a dimer in which both subunits contribute to the active site. Moreover, superposition of the ANT(6)\u2010Ib structure with the structurally related enzyme lincosamide nucleotidyltransferase B (LinB) permitted the identification of a putative nucleotide binding site. These data also suggest that residues D44 and D46 coordinate essential divalent metal ions and D102 functions as the catalytic base.\n                  <\/jats:p>","DOI":"10.1002\/prot.26745","type":"journal-article","created":{"date-parts":[[2024,9,9]],"date-time":"2024-09-09T04:23:49Z","timestamp":1725855829000},"page":"413-419","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Structural and Biochemical Characterization of Aminoglycoside Nucleotidyltransferase(6)\u2010Ib From\n                    <i>Campylobacter fetus<\/i>\n                    subsp.\n                    <i>fetus<\/i>"],"prefix":"10.1002","volume":"93","author":[{"given":"Pranav","family":"Nalam","sequence":"first","affiliation":[{"name":"Department of Chemistry Grand Valley State University  Allendale Michigan USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7286-2860","authenticated-orcid":false,"given":"Paul D.","family":"Cook","sequence":"additional","affiliation":[{"name":"Department of Chemistry Grand Valley State University  Allendale Michigan USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-1743-5273","authenticated-orcid":false,"given":"Brian A.","family":"Smith","sequence":"additional","affiliation":[{"name":"Department of Chemistry Grand Valley State University  Allendale Michigan 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