Conformational Domain Changes in Cas9 (IMAGE)

University of California - Berkeley

Conformational Domain Changes in Cas9

Caption

The Cas9 protein (gray) is an RNA-guided nuclease that can be programmed to bind and cut any matching DNA sequence (dark blue double helix), making it a powerful tool for genome engineering. Upon target binding, Cas9 protein domains undergo conformational rearrangements (the motions of individual amino acids are represented by rocket tails) to activate the Cas9-sgRNA complex for target cleavage. The REC3 domain (teal) is responsible for target sensing, which signals the outward rotation of the REC2 domain (magenta) to open a path for the HNH nuclease domain (yellow). This active conformation of Cas9 is then capable of triggering concerted cleavage of both strands of the target DNA.

Credit

Janet Iwasa graphic for Doudna Lab

Usage Restrictions

None

License

Licensed content

Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.