Protein linkers provide limits on the domain interactions in the ABC importer GlnPQ and determine the rate of transportSchuurman-Wolters, G. K., de Boer, M., Pietrzyk, M. K. & Poolman, B., 13-Apr-2018, In : Journal of Molecular Biology. p. 1249-1262 14 p., j.jmb.2018.02.014.
Research output: Contribution to journal › Article › Academic › peer-review
GlnPQ is an ATP-Binding Cassette (ABC) importer with a unique domain organization and intricate transport behaviour. The protein has two extracytoplamic substrate-binding domains (SBDs) per membrane subunit, each with different specificity for amino acids and different spacing to the translocator domain. We determined the effect of the length and structure of the linkers, which connect the SBDs to each other and to the membrane-embedded translocator domain, on the transport by GlnPQ. We reveal that varying the linker length impacts transport in a dual manner that depends on the conformational dynamics of the SBD. Varying the linker length not only changes the time for the SBD to find the translocator (docking), it additionally changes the probability to release the substrate again, thus altering the transport efficiency. On the basis of the experimental data and mathematical modelling, we calculate the docking efficiency as function of linker length and lifetime of the closed conformation. Importantly, not only linker length but also features in the sequence are important for efficient delivery of substrate from SBD to the translocator. We show that the linkers provide a platform for SBD docking and are not merely flexible structures.
|Number of pages||14|
|Journal||Journal of Molecular Biology|
|Publication status||Published - 13-Apr-2018|
- ABC transporter, amino acid uptake, inter-domain interactions, muti-domain protein complexes, substrate-binding protein, transport efficiency, protein linker insertion