ArticleProtein science : a publication of the Protein Society1996
The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Characterizing the Conformational Dynamics of the Ribose Transporter B Protein inJournal of chemical theory and computation · 2026Article
- Disorders of gut microbiota in children with Tetralogy of Fallot.Translational pediatrics · 2022Article
- Whole genome analysis for plant growth promotion profiling ofFrontiers in microbiology · 2022Article
- Enhanced acid-stress tolerance in Lactococcus lactis NZ9000 by overexpression of ABC transporters.Microbial cell factories · 2019Article
- High-throughput, signature-tagged mutagenic approach to identify novel virulence factors of Yersinia pestis CO92 in a mouse model of infection.Infection and immunity · 2015Article
- In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.The Journal of biological chemistry · 2015Article
- The motor domains of ABC-transporters. What can structures tell us?Naunyn-Schmiedeberg's archives of pharmacology · 2006Review
- Topology of RbsC, the membrane component of the Escherichia coli ribose transporter.Journal of bacteriology · 2003Article
- Linkage map of Escherichia coli K-12, edition 10: the traditional map.Microbiology and molecular biology reviews : MMBR · 1998Review
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
The nucleotide-binding component of the high-affinity ribose transport system of Escherichia coli, RbsA, was overproduced from a T7-7 expression vector, and the protein was purified. Biochemical analyses of the purified protein indicated that the ATP analogues, 5'-FSBA and 8-azido ATP, covalently labeled the protein, a reaction that was inhibited by ATP, but not by GTP or CTP. The pure protein exhibited low-level ATPase activity with a K(m) of about 140 microM. Analyses of bacterial strains carrying chromosomal deletions of rbsA and other rbs genes suggested that RbsA is important for the chemotaxis function, a surprising result that was not anticipated from previous studies. However, an inconsistency between the several results from deletion strains raises questions regarding the interpretations of the in vivo data.
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