Responses to Ligand Binding in the Bacterial DNA Sliding Clamp "β-Clamp" Manifest in Dynamic Allosteric Effects.

ABSTRACT: The homo-dimeric, ring-shaped bacterial DNA sliding clamp, β-clamp, is a central hub in DNA replication and repair. It interacts with a plethora of proteins via their short linear motifs, binding to the same hydrophobic binding pocket on β-clamp. Although the structure, functions, and interactions of β-clamp have been amply studied, less focus has been on understanding its dynamics and how this is influenced by ligand binding. In this work, we have made a backbone nuclear magnetic resonance (NMR) assignment of the 83 kDa dimeric β-clamp and used NMR in combination with hydrogen-deuterium exchange mass spectrometry to scrutinize the dynamics of β-clamp and how ligand binding affects this. We found that the binding of a short peptide from the polymerase III α subunit affects the dynamics and

SUBMITTER: Simonsen S 

PROVIDER: S-EPMC12594201 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature