{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T18:54:49Z","timestamp":1791485689488,"version":"4.3.4"},"reference-count":43,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2019,3,4]],"date-time":"2019-03-04T00:00:00Z","timestamp":1551657600000},"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":["Protein Science"],"published-print":{"date-parts":[[2019,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Members of the ATP\u2010binding cassette F (ABC\u2010F) proteins confer resistance to several classes of clinically important antibiotics through ribosome protection. Recent structures of two ABC\u2010F proteins, <jats:styled-content style=\"fixed-case\"><jats:italic>Pseudomonas aeruginosa<\/jats:italic><\/jats:styled-content> MsrE and <jats:italic>Bacillus subtilis<\/jats:italic> VmlR bound to ribosome have shed light onto the ribosome protection mechanism whereby drug resistance is mediated by the antibiotic resistance domain (ARD) connecting the two ATP binding domains. ARD of the E site bound MsrE and VmlR extends toward the drug binding region within the peptidyl transferase center (PTC) and leads to conformational changes in the P site tRNA acceptor stem, the PTC, and the drug binding site causing the release of corresponding drugs. The structural similarities and differences of the MsrE and VmlR structures likely highlight an universal ribosome protection mechanism employed by antibiotic resistance (ARE) ABC\u2010F proteins. The variable ARD domains enable this family of proteins to adapt the protection mechanism for several classes of ribosome\u2010targeting drugs. ARE ABC\u2010F genes have been found in numerous pathogen genomes and multi\u2010drug resistance conferring plasmids. Collectively they mediate resistance to a broader range of antimicrobial agents than any other group of resistance proteins and play a major role in clinically significant drug resistance in pathogenic bacteria. Here, we review the recent structural and biochemical findings on these emerging resistance proteins, offering an update of the molecular basis and implications for overcoming ABC\u2010F conferred drug resistance.<\/jats:p>","DOI":"10.1002\/pro.3589","type":"journal-article","created":{"date-parts":[[2019,2,12]],"date-time":"2019-02-12T09:38:47Z","timestamp":1549964327000},"page":"684-693","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":58,"title":["Ribosome protection by ABC\u2010F proteins\u2014Molecular mechanism and potential drug design"],"prefix":"10.1002","volume":"28","author":[{"given":"Rya","family":"Ero","sequence":"first","affiliation":[{"name":"School of Biological Sciences, Nanyang Technological University  60 Nanyang Drive Singapore 637551"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Veerendra","family":"Kumar","sequence":"additional","affiliation":[{"name":"A*STAR (Agency for Science, 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