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Bacillus subtilis MutL samples multiple conformations during nucleotide binding and hydrolysis
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DOI：10.1016/j.str.2025.12.007.png)
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Abstract
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• MutL proteins with nuclease activity bind ATP with lower affinity than those without • The ATPase domains of Bacillus subtilis MutL do not associate stably • BsMutL samples the same conformational landscape as EcMutL • Bacterial MutL proteins sample similar conformations but show different dynamics
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