ArticleJournal of bacteriology2001
Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 14 citations in OpenAlex.
- Binding Protein-Dependent Uptake of Maltose into Cells via an ATP-Binding Cassette Transporter.EcoSal Plus · 2010Article
- Structural insights into ABC transporter mechanism.Current opinion in structural biology · 2008Review
- Structure, function, and evolution of bacterial ATP-binding cassette systems.Microbiology and molecular biology reviews : MMBR · 2008Review
- An integrated transport mechanism of the maltose ABC importer.Research in microbiologyReview
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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