{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,5]],"date-time":"2026-04-05T13:52:48Z","timestamp":1775397168949,"version":"3.50.1"},"reference-count":0,"publisher":"Proceedings of the National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1979,12]]},"abstract":"<jats:p>A protein isolated from Escherichia coli complements the DNA gyrase A (NalA) protein to generate an activity that relaxes supercoiled DNA. Oxolinic acid, a known inhibitor of DNA gyrase, blocks this activity and causes double-strand cleavage of DNA at the same sites as are attacked by DNA gyrase. The protein, of molecular weight 50,000, appears to be fragment of the DNA gyrase B (Cou) protein (molecular weight, 90,000) as judged by the identical sizes of numerous peptides produced by partial proteolytic digestion. The complex of this fragment and the gyrase A protein lacks both the DNA-supercoiling and DNA-dependent ATPase activities of DNA gyrase.<\/jats:p>","DOI":"10.1073\/pnas.76.12.6289","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T07:53:20Z","timestamp":1149062000000},"page":"6289-6293","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":122,"title":["DNA gyrase: purification and catalytic properties of a fragment of gyrase B protein."],"prefix":"10.1073","volume":"76","author":[{"given":"M","family":"Gellert","sequence":"first","affiliation":[]},{"given":"L M","family":"Fisher","sequence":"additional","affiliation":[]},{"given":"M H","family":"O'Dea","sequence":"additional","affiliation":[]}],"member":"341","published-online":{"date-parts":[[1979,12]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.76.12.6289","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T14:55:01Z","timestamp":1649861701000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.76.12.6289"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1979,12]]},"references-count":0,"journal-issue":{"issue":"12","published-print":{"date-parts":[[1979,12]]}},"alternative-id":["10.1073\/pnas.76.12.6289"],"URL":"https:\/\/doi.org\/10.1073\/pnas.76.12.6289","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1979,12]]},"assertion":[{"value":"1979-12-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}