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Publication Abstract from PubMed

The adenosine triphosphate (ATP)-binding cassette (ABC) importer GlnPQ from Lactococcus lactis has two sequential covalently linked substrate-binding domains (SBDs), which capture the substrates and deliver them to the translocon. The two SBDs differ in their ligand specificities, binding affinities and the distance to the transmembrane domain; interestingly, both SBDs can bind their ligands simultaneously without affecting each other. In this work, we studied the binding of ligands to both SBDs using X-ray crystallography and molecular dynamics simulations. We report three high-resolution structures of SBD1, namely, the wild-type SBD1 with bound asparagine or arginine, and E184D SBD1 with glutamine bound. Molecular dynamics (MD) simulations provide a detailed insight into the dynamics associated with open-closed transitions of the SBDs.

Exploring the Ligand Binding and Conformational Dynamics of the Substrate-Binding Domain 1 of the ABC Transporter GlnPQ.,Nemchinova M, Schuurman-Wolters GK, Whittaker JJ, Arkhipova V, Marrink SJ, Poolman B, Guskov A J Phys Chem B. 2024 Aug 15;128(32):7822-7832. doi: 10.1021/acs.jpcb.4c02662. Epub , 2024 Aug 1. PMID:39090964^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.