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[2018] Solution structure and dynamics of Xanthomonas albilineans Cas2 provide mechanistic insight on nuclease activity
작성일
2023-02-03
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53


[2018] Solution structure and dynamics of Xanthomonas albilineans Cas2 provide mechanistic insight on nuclease activity

Journal
FEBS Lett 592(1): 147-155

Authors
Jeong, M., Kim, I., Kim, G., Ka, D., Kim, N.K., Bae, E., Ryu, K.S. and Suh, J.Y.*
*Denotes Corresponding Author

Abstract
Cas2 protein in the CRISPR-Cas system functions as a scaffold for the acquisition of foreign DNA fragments, and as a nuclease against DNA and RNA substrates. Crystal structures of Cas2 have shown catalytically inactive conformational states that do not explain the mechanism of Cas2 nuclease activity. Here, we report that Xanthomonas albilineans Cas2 (XaCas2) assumes an inactive conformation in solution. Residual dipolar couplings and NMR relaxation, however, provide direct evidence on conformational dynamics at the predicted hinge region. Furthermore, XaCas2 transiently associates with metal ions for nuclease activity via highly mobile Asp8. Taken together, the dual function of Cas2 can be explained by a dynamic equilibrium of conformational states that serve as a scaffold or as a nuclease on demand.

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doi: 10.1002/1873-3468.12942
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