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Published in

American Society for Microbiology, Journal of Bacteriology, 1(183), p. 375-381, 2001

DOI: 10.1128/jb.183.1.375-381.2001

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Characterization of Transmembrane Segments 3, 4, and 5 of MalF by Mutational Analysis

Journal article published in 2001 by Angelika Steinke, Sandra Grau, Amy Davidson, Eckhard Hofmann ORCID, Michael Ehrmann
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

ABSTRACT MalF and MalG are the cytoplasmic membrane components of the binding protein-dependent ATP binding cassette maltose transporter in Escherichia coli . They are thought to form the transport channel and are thus of critical importance for the mechanism of transport. To study the contributions of individual transmembrane segments of MalF, we isolated 27 point mutations in membrane-spanning segments 3, 4, and 5. These data complement a previous study, which described the mutagenesis of membrane-spanning segments 6, 7, and 8. While most of the isolated mutations appear to cause assembly defects, L 323 Q in helix 5 could interfere more directly with substrate specificity. The phenotypes and locations of the mutations are consistent with a previously postulated structural model of MalF.