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Conformational changes of DNA repair glycosylase MutM triggered by DNA binding

DOI: 10.1002/1873-3468.13876 DOI Help

Authors: Barbora Landová (Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences) , Jan Silhan (Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters , VOL 38

State: Published (Approved)
Published: July 2020

Abstract: Bacterial MutM is a DNA repair glycosylase removing DNA damage generated from oxidative stress and, therefore, preventing mutations and genomic instability. MutM belongs to the Fpg/Nei family of prokaryotic enzymes sharing structural and functional similarities with their eukaryotic counterparts, for example, NEIL1–NEIL3. Here, we present two crystal structures of MutM from pathogenic Neisseria meningitidis: a MutM holoenzyme and MutM bound to DNA. The free enzyme exists in an open conformation, while upon binding to DNA, both the enzyme and DNA undergo substantial structural changes and domain rearrangement. Our data show that not only NEI glycosylases but also the MutMs undergo dramatic conformational changes. Moreover, crystallographic data support the previously published observations that MutM enzymes are rather flexible and dynamic molecules.

Journal Keywords: base excision DNA repair; DNA repair; Fpg/Nei; MutM; Neisseria meningitidis

Diamond Keywords: Bacteria

Subject Areas: Chemistry, Biology and Bio-materials

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: 14.1 at BESSYII

Added On: 21/09/2020 14:12

Discipline Tags:

Pathogens Health & Wellbeing Biochemistry Genetics Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)