Explore the words cloud of the VisTrans project. It provides you a very rough idea of what is the project "VisTrans" about.
The following table provides information about the project.
THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE
|Coordinator Country||United Kingdom [UK]|
|Total cost||2˙208˙618 €|
|EC max contribution||2˙208˙618 € (100%)|
1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
|Duration (year-month-day)||from 2017-09-01 to 2022-08-31|
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|1||THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE||UK (CAMBRIDGE)||coordinator||2˙208˙618.00|
The project will investigate multi-component molecular machines that drive substrates across the cell envelope of bacteria. Some of the machines pump antibiotics or toxins, and so contribute to drug resistance and virulence in pathogenic strains. Questions that will be addressed include what the molecular pumps look like, how they are assembled and regulated, how they capture and translocate substrates, and the stereochemical basis for the cooperative switching of substrate-binding states. Molecular pumps that will be studied include tripartite systems driven by ATP hydrolysis, which play a central role in the efflux of macrolide antibiotics and secretion of toxins in Gram-negative bacteria, and those that use secondary transporters energized by electrochemical gradients. We will build upon our earlier observations to prepare a series of intermediates encompassing the key steps in the transport processes, to visualize tertiary and quaternary structural changes, the pathway of substrates in the efflux pumps, and the threading of toxin polypeptides through the constricted channel in the secretion assembly. The pumps and secretion systems cycle through intermediate states, and these will be studied at high resolution by cryoEM and crystallography to understand how the conformational states switch with strong cooperativity and avoid futile cycles that dissipate energy. Our work indicates that the activity of these transporters can be modulated by small peptides and potential co-factors, and we will address how these work. The project will build on our novel approach to engineer the pump assemblies that enables structural analysis at high resolution in isolation and in situ, and will be complemented with mechanistic analyses in vitro and in vivo. The project will deliver a comprehensive, structure-based description of the mechanism of drug efflux and protein translocation by transport machines and their regulation in diverse pathogenic bacteria.
|year||authors and title||journal||last update|
Dijun Du, Xuan Wang-Kan, Arthur Neuberger, Hendrik W. van Veen, Klaas M. Pos, Laura J. V. Piddock, Ben F. Luisi
Multidrug efflux pumps: structure, function and regulation
published pages: 523-539, ISSN: 1740-1526, DOI: 10.1038/s41579-018-0048-6
|Nature Reviews Microbiology 16/9||2020-01-28|
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The information about "VISTRANS" are provided by the European Opendata Portal: CORDIS opendata.
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