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Molecular Microbiology
In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli : modulation by ATP1998 •
1995 •
Biochimica et Biophysica Acta (BBA) - Biomembranes
ATP-binding cassette transporters in Escherichia coli2008 •
2000 •
Journal of Biological Chemistry
Substrate Transport Activation Is Mediated through Second Periplasmic Loop of Transmembrane Protein MalF in Maltose Transport Complex of Escherichia coli2012 •
Proceedings of the …
The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter2002 •
Fems Microbiology Reviews
The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea2001 •
Until recently, extracytoplasmic solute receptor (ESR)-dependent uptake systems were invariably found to possess a conserved ATP-binding protein (the ATP-binding cassette protein or ABC protein), which couples ATP hydrolysis to the translocation of the solute across the cytoplasmic membrane. While it is clear that this class of ABC transporter is ubiquitous in prokaryotes, it is now firmly established that other, unrelated types of membrane transport systems exist which also have ESR components. These systems have been designated tripartite ATP-independent periplasmic (TRAP) transporters, and they form a distinct class of ESR-dependent secondary transporters where the driving force for solute accumulation is an electrochemical ion gradient and not ATP hydrolysis. Currently, the most well characterised TRAP transporter at the functional and molecular level is the high-affinity C4-dicarboxylate transport (Dct) system from Rhodobacter capsulatus. This consists of three proteins; an ESR (DctP) and small (DctQ) and large (DctM) integral membrane proteins. The characteristics of this system are discussed in detail. Homologues of the R. capsulatus DctPQM proteins are present in a diverse range of prokaryotes, both bacteria and archaea, but not in eukaryotes. The deduced structures and possible functions of these homologous systems are described. In addition to the DctP family, other types of ESRs can be associated with TRAP transporters. A conserved family of immunogenic extracytoplasmic proteins is shown to be invariably associated with TRAP systems that contain a large DctQM fusion protein. All of the currently known archaeal systems are of this type. It is concluded that TRAP transporters are a widespread and ancient type of solute uptake system that transport a potentially diverse range of solutes and most likely evolved by the addition of auxiliary proteins to a single secondary transporter.
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2020 •
2017 •
Perspectives in Science
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The Right to the Continuous Improvement of Living Conditions
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Effect of moisture on the viscoelastic properties of an epoxy-clay nanocomposite2011 •
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2018 •
1981 •