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Abstract
PAM recognition induces an allosteric mechanism in Cas9 that facilitates DNA cleavage.
- PAM binding is crucial for the Cas9 endonuclease to generate double strand breaks in DNA.
- Microsecond molecular dynamics simulations provide evidence for the allosteric mechanism activated by PAM.
- PAM functions as an allosteric effector, influencing the conformational changes in the Cas9 catalytic domains.
- The interdependent dynamics of the HNH and RuvC domains are essential for the coordinated cleavage of both DNA strands.
- Targeting this allosteric mechanism may offer a way to control the functionality of CRISPR-Cas9.
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