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Journal Article

Membrane-anchored substrate binding proteins are deployed in secondary TAXI transporters.

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Geertsma,  Eric R
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Roden, A., Engelin, M. K., Pos, K. M., & Geertsma, E. R. (2023). Membrane-anchored substrate binding proteins are deployed in secondary TAXI transporters. Biological chemistry, 404(7), 715-725. doi:10.1515/hsz-2022-0337.


Cite as: https://hdl.handle.net/21.11116/0000-000E-AB14-B
Abstract
Substrate-binding proteins (SBPs) are part of solute transport systems and serve to increase substrate affinity and uptake rates. In contrast to primary transport systems, the mechanism of SBP-dependent secondary transport is not well understood. Functional studies have thus far focused on Na+-coupled Tripartite ATP-independent periplasmic (TRAP) transporters for sialic acid. Herein, we report the in vitro functional characterization of TAXIPm-PQM from the human pathogen Proteus mirabilis. TAXIPm-PQM belongs to a TRAP-subfamily using a different type of SBP, designated TRAP-associated extracytoplasmic immunogenic (TAXI) protein. TAXIPm-PQM catalyzes proton-dependent α-ketoglutarate symport and its SBP is an essential component of the transport mechanism. Importantly, TAXIPm-PQM represents the first functionally characterized SBP-dependent secondary transporter that does not rely on a soluble SBP, but uses a membrane-anchored SBP instead.