{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T11:15:57Z","timestamp":1758280557002,"version":"3.37.3"},"reference-count":70,"publisher":"Portland Press Ltd.","issue":"2","license":[{"start":{"date-parts":[[2020,1,10]],"date-time":"2020-01-10T00:00:00Z","timestamp":1578614400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/2.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2020,1,31]]},"abstract":"<jats:p>Acyl carrier proteins (ACPs) are small helical proteins found in all kingdoms of life, primarily involved in fatty acid and polyketide biosynthesis. In eukaryotes, ACPs are part of the fatty acid synthase (FAS) complex, where they act as flexible tethers for the growing lipid chain, enabling access to the distinct active sites in FAS. In the type II synthesis systems found in bacteria and plastids, these proteins exist as monomers and perform various processes, from being a donor for synthesis of various products such as endotoxins, to supplying acyl chains for lipid A and lipoic acid FAS (quorum sensing), but also as signaling molecules, in bioluminescence and activation of toxins. The essential and diverse nature of their functions makes ACP an attractive target for antimicrobial drug discovery. Here, we report the structure, dynamics and evolution of ACPs from three human pathogens: Borrelia burgdorferi, Brucella melitensis and Rickettsia prowazekii, which could facilitate the discovery of new inhibitors of ACP function in pathogenic bacteria.<\/jats:p>","DOI":"10.1042\/bcj20190797","type":"journal-article","created":{"date-parts":[[2020,1,10]],"date-time":"2020-01-10T12:22:13Z","timestamp":1578658933000},"page":"491-508","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Comparative structure, dynamics and evolution of acyl-carrier proteins from <i>Borrelia burgdorferi<\/i>, <i>Brucella melitensis<\/i> and <i>Rickettsia prowazekii<\/i>"],"prefix":"10.1042","volume":"477","author":[{"given":"Ravi P.","family":"Barnwal","sequence":"first","affiliation":[{"name":"Department of Biophysics, Panjab University, Chandigarh 160014, India"},{"name":"Department of Chemistry, University of Washington, Seattle 98195, WA, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mandeep","family":"Kaur","sequence":"additional","affiliation":[{"name":"Department of Biophysics, Panjab University, Chandigarh 160014, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alec","family":"Heckert","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Washington, Seattle 98195, WA, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Janeka","family":"Gartia","sequence":"additional","affiliation":[{"name":"Center for Interdisciplinary Sciences, Tata Institute of Fundamental Research, Gopanpally, Hyderabad 500075, India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6642-7144","authenticated-orcid":false,"given":"Gabriele","family":"Varani","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Washington, Seattle 98195, WA, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2020,1,31]]},"reference":[{"key":"2021112218051740000_BCJ-2019-0797C1","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1038\/nature12810","article-title":"Trapping the dynamic acyl carrier protein in fatty acid biosynthesis","volume":"505","year":"2014","journal-title":"Nature"},{"key":"2021112218051740000_BCJ-2019-0797C2","doi-asserted-by":"publisher","first-page":"422","DOI":"10.1038\/nature12679","article-title":"Chasing acyl carrier protein through a catalytic cycle of lipid A production","volume":"505","year":"2014","journal-title":"Nature"},{"key":"2021112218051740000_BCJ-2019-0797C3","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1126\/science.1138249","article-title":"Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase","volume":"316","year":"2007","journal-title":"Science"},{"key":"2021112218051740000_BCJ-2019-0797C4","doi-asserted-by":"publisher","first-page":"1315","DOI":"10.1126\/science.1161269","article-title":"The crystal structure of a mammalian fatty acid synthase","volume":"321","year":"2008","journal-title":"Science"},{"key":"2021112218051740000_BCJ-2019-0797C5","doi-asserted-by":"publisher","first-page":"373","DOI":"10.1017\/S0033583510000156","article-title":"Structure and function of eukaryotic fatty acid synthases","volume":"43","year":"2010","journal-title":"Q. 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