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- W3104438892 abstract "Abstract McrBC complexes are motor-driven nucleases functioning in bacterial self-defense by cleaving foreign DNA. The GTP-specific AAA + protein McrB powers translocation along DNA and its hydrolysis activity is stimulated by its partner nuclease McrC. Here, we report cryo-EM structures of Thermococcus gammatolerans McrB and McrBC, and E. coli McrBC. The McrB hexamers, containing the necessary catalytic machinery for basal GTP hydrolysis, are intrinsically asymmetric. This asymmetry directs McrC binding so that it engages a single active site, where it then uses an arginine/lysine-mediated hydrogen-bonding network to reposition the asparagine in the McrB signature motif for optimal catalytic function. While the two McrBC complexes use different DNA-binding domains, these contribute to the same general GTP-recognition mechanism employed by all G proteins. Asymmetry also induces distinct inter-subunit interactions around the ring, suggesting a coordinated and directional GTP-hydrolysis cycle. Our data provide insights into the conserved molecular mechanisms governing McrB family AAA + motors." @default.
- W3104438892 created "2020-11-23" @default.
- W3104438892 creator A5002113575 @default.
- W3104438892 creator A5053000248 @default.
- W3104438892 creator A5059152784 @default.
- W3104438892 creator A5085742847 @default.
- W3104438892 creator A5085977723 @default.
- W3104438892 date "2020-11-20" @default.
- W3104438892 modified "2023-10-18" @default.
- W3104438892 title "Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes" @default.
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