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Structure-based mechanism for activation of the AAA plus GTPase McrB by the endonuclease McrC
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab). Karolinska Institutet, Sweden.
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Number of Authors: 72019 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 10, article id 3058Article in journal (Refereed) Published
Abstract [en]

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 angstrom 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 gamma subunit complexed to alpha(3)beta(3) of F-1-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.

Place, publisher, year, edition, pages
2019. Vol. 10, article id 3058
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Biological Sciences
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URN: urn:nbn:se:su:diva-171743DOI: 10.1038/s41467-019-11084-1ISI: 000474824300005PubMedID: 31296862OAI: oai:DiVA.org:su-171743DiVA, id: diva2:1349474
Available from: 2019-09-09 Created: 2019-09-09 Last updated: 2019-09-09Bibliographically approved

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