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Updated: Jan 7, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Bacillus subtilis MutL samples multiple conformations during nucleotide binding and hydrolysis.

Javier Rodríguez González¹, Corey L Davis², Hunter Wilkins²

¹Department of Biochemistry and Centre de Recherche en Biologie Structurale, McGill University, Montreal, QC, Canada.

Structure (London, England : 1993)

|January 1, 2026

Summary

This summary is machine-generated.

DNA mismatch repair proteins MutL function asymmetrically. Bacillus subtilis MutL

Keywords:

DNA mismatch repair GHKL ATPases MutL X-ray crystallography atomic force microscopy conformational changes protein dynamics transient protein interactions

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Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

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Published on: March 16, 2022

Area of Science:

Molecular biology
Genetics
Biochemistry

Background:

DNA mismatch repair (MMR) corrects replication errors to maintain genome stability.
MutS and MutL proteins are key conserved components of the MMR pathway.
The asymmetric function of bacterial MutS in mismatch recognition is established, but MutL's role is less understood.

Purpose of the Study:

To investigate the ATPase domain of Bacillus subtilis MutL, an endonuclease-active MutL homolog.
To compare B. subtilis MutL with the endonuclease-inactive Escherichia coli MutL.
To explore the conformational dynamics and ATP binding of B. subtilis MutL.

Main Methods:

Biochemical characterization of the ATPase domain of B. subtilis MutL.
Comparative analysis of B. subtilis MutL and E. coli MutL.
Conformational analysis using techniques sensitive to protein structure.

Main Results:

B. subtilis MutL exhibits low affinity for ATP.
B. subtilis MutL samples diverse conformations, similar to eukaryotic MutL paralogs.
These conformations are linked to ATP-induced dimer compaction and nuclease activity.

Conclusions:

B. subtilis MutL's conformational flexibility is crucial for its endonuclease activity.
The findings suggest a conserved mechanism of MutL function across species.
Asymmetric MutL function may be linked to ATP-dependent conformational changes and nuclease activation.