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

The cell surface of Gram-negative bacteria contains lipopolysaccharides (LPS), which provide a barrier against the entry of many antibiotics. LPS assembly involves a multiprotein LPS transport (Lpt) complex that spans from the cytoplasm to the outer membrane. In this complex, an unusual ATP-binding...

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Bibliographic Details

Published in:	Proceedings of the National Academy of Sciences - PNAS 2014-04, Vol.111 (13), p.4982-4987
Main Authors:	Sherman, David J., Lazarus, Michael B., Murphy, Lea, Liu, Charles, Walker, Suzanne, Ruiz, Natividad, Kahne, Daniel
Format:	Article
Language:	eng
Subjects:	Active sites Adenosine Diphosphate - metabolism Adenosine triphosphatase Adenosine triphosphatases Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Amino Acids - metabolism Antibiotics ATP binding cassette transporters ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - metabolism Binding sites Biocatalysis Biochemistry Biological Sciences Biological Transport Catalytic Domain Cell Membrane - metabolism Cells Crystal structure Crystallography, X-Ray Cytoplasm Enzyme kinetics Escherichia coli Escherichia coli - enzymology Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Gram-negative bacteria Hydrolysis Lipopolysaccharides Lipopolysaccharides - metabolism Microbial Viability Models, Molecular Molecules Mutant Proteins - chemistry Mutant Proteins - metabolism P branes Protein Binding Protein Structure, Secondary
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