Characterization of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA.

ABSTRACT: MsbA is a member of the ABC transporter superfamily that is specifically found in Gram-negative bacteria and is homologous to proteins involved in both bacterial and human drug resistance. The E506Q and H537A mutations have been introduced and used for crystallization of other members of the ABC transporter protein family, including BmrA and the ATPase domains MalK, HlyB-NBD, and MJ0796, but have not been previously studied in detail or investigated in the MsbA lipid A exporter. We utilized an array of biochemical and EPR spectroscopy approaches to characterize the local and global effects of these nucleotide binding domain mutations on the E. coli MsbA homodimer. The lack of cell viability in an in vivo growth assay confirms that the presence of the E506Q or H537A mutations within MsbA cr

SUBMITTER: Schultz KM 

PROVIDER: S-EPMC3128438 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature