Inherent backbone dynamics fine-tune the functional plasticity of Tudor domains.

Kawale AA, Burmann BM

Structure 29 (11) 1253-1265.e4 [2021-11-04; online 2021-06-30]

Tudor domains are crucial for mediating a diversity of protein-protein or protein-DNA interactions involved in nucleic acid metabolism. Using solution NMR spectroscopy, we assess the comprehensive understanding of the dynamical properties of the respective Tudor domains from four different bacterial (Escherichia coli) proteins UvrD, Mfd, RfaH, and NusG involved in different aspects of bacterial transcription regulation and associated processes. These proteins are benchmarked to the canonical Tudor domain fold from the human SMN protein. The detailed analysis of protein backbone dynamics and subsequent analysis by the Lipari-Szabo model-free approach revealed subtle differences in motions of the amide-bond vector on both pico- to nanosecond and micro- to millisecond timescales. On these timescales, our comparative approach reveals the usefulness of discrete amplitudes of dynamics to discern the different functionalities for Tudor domains exhibiting promiscuous binding, including the metamorphic Tudor domain included in the study.

Swedish NMR Centre (SNC) [Service]

PubMed 34197736

DOI 10.1016/j.str.2021.06.007

Crossref 10.1016/j.str.2021.06.007

pii: S0969-2126(21)00211-2

Publications 9.5.0