Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport

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Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport

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Title: Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport
Author: Sherman, David Joseph; Lazarus, Michael B.; Murphy, Lea; Liu, Charles Xin; Kahne, Suzanne Walker; Ruiz, Natividad; Kahne, Daniel

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Citation: Sherman, David J., Michael B. Lazarus, Lea Murphy, Charles Liu, Suzanne Walker, Natividad Ruiz, and Daniel Kahne. 2014. “Decoupling Catalytic Activity from Biological Function of the ATPase That Powers Lipopolysaccharide Transport.” Proc Natl Acad Sci USA 111 (13) (March 17): 4982–4987. doi:10.1073/pnas.1323516111.
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Abstract: Gram-negative bacteria contain an unusual outer membrane that prevents the entry of most currently available antibiotics. This membrane contains a complex glycolipid, LPS, on the exterior. It is not understood how such a large molecule, which can contain hundreds of sugars and six fatty acyl chains, is transported across the cell envelope from its site of synthesis in the cytoplasmic membrane to the cell surface. Using a combination of genetics, biochemistry, and structural biology, we characterized residues in the protein that powers LPS transport to gain mechanistic insight into how ATP hydrolysis is coupled to the biological function of the transporter. These tools help us understand how to design antibiotics targeting this essential pathway.
Published Version: doi:10.1073/pnas.1323516111
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3977253/
Terms of Use: This article is made available under the terms and conditions applicable to Open Access Policy Articles, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#OAP
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:23597719
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