8B5E

Exploring the ligand binding and conformational dynamics of receptor domain 1 of the ABC transporter GlnPQ

Summary for 8B5E

• Entry DOI: 10.2210/pdb8b5e/pdb
• Descriptor: ABC transporter permease subunit, ARGININE, SODIUM ION, ... (7 entities in total)
• Functional Keywords: transporter, membrane protein, transport protein
• Biological source: Lactococcus lactis
• Total number of polymer chains: 2
• Total formula weight: 50185.56

Authors

Whittaker, J.,Guskov, A. (deposition date: 2022-09-22, release date: 2023-10-04, Last modification date: 2024-09-04)

Primary citation

Nemchinova, M.,Schuurman-Wolters, G.K.,Whittaker, J.J.,Arkhipova, V.,Marrink, S.J.,Poolman, B.,Guskov, A.
Exploring the Ligand Binding and Conformational Dynamics of the Substrate-Binding Domain 1 of the ABC Transporter GlnPQ.
J.Phys.Chem.B, 128:7822-7832, 2024

PubMed Abstract: The adenosine triphosphate (ATP)-binding cassette (ABC) importer GlnPQ from 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.

PubMed: 39090964
DOI: 10.1021/acs.jpcb.4c02662

Experimental method

X-RAY DIFFRACTION (1.6 Å)