Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC

Neha Nirwan, Yuzuru Itoh, Pratima Singh, Sutirtha Bandyopadhyay, Kutti R. Vinothkumar, Alexey Amunts () and Kayarat Saikrishnan ()
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Neha Nirwan: Indian Institute of Science Education and Research
Yuzuru Itoh: Stockholm University
Pratima Singh: Indian Institute of Science Education and Research
Sutirtha Bandyopadhyay: Indian Institute of Science Education and Research
Kutti R. Vinothkumar: MRC Laboratory of Molecular Biology
Alexey Amunts: Stockholm University
Kayarat Saikrishnan: Indian Institute of Science Education and Research

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: Abstract The AAA+ GTPase McrB powers DNA cleavage by the endonuclease McrC. The GTPase itself is activated by McrC. The architecture of the GTPase and nuclease complex, and the mechanism of their activation remained unknown. Here, we report a 3.6 Å structure of a GTPase-active and DNA-binding deficient construct of McrBC. Two hexameric rings of McrB are bridged by McrC dimer. McrC interacts asymmetrically with McrB protomers and inserts a stalk into the pore of the ring, reminiscent of the γ subunit complexed to α3β3 of F1-ATPase. Activation of the GTPase involves conformational changes of residues essential for hydrolysis. Three consecutive nucleotide-binding pockets are occupied by the GTP analogue 5’-guanylyl imidodiphosphate and the next three by GDP, which is suggestive of sequential GTP hydrolysis.

Date: 2019
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DOI: 10.1038/s41467-019-11084-1

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