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CryoEM structure of human CMG bound to ATPgammaS and DNA

ABSTRACT:

SUBMITTER: Neil James Rzechorzek

PROVIDER: EMPIAR-10471 | biostudies-other |

REPOSITORIES: biostudies-other

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CryoEM structures of human CMG-ATPγS-DNA and CMG-AND-1 complexes.

Rzechorzek Neil J NJ Hardwick Steven W SW Jatikusumo Vincentius A VA Chirgadze Dimitri Y DY Pellegrini Luca L

Nucleic acids research 20200701 12

DNA unwinding in eukaryotic replication is performed by the Cdc45-MCM-GINS (CMG) helicase. Although the CMG architecture has been elucidated, its mechanism of DNA unwinding and replisome interactions remain poorly understood. Here we report the cryoEM structure at 3.3 Å of human CMG bound to fork DNA and the ATP-analogue ATPγS. Eleven nucleotides of single-stranded (ss) DNA are bound within the C-tier of MCM2-7 AAA+ ATPase domains. All MCM subunits contact DNA, from MCM2 at the 5'-end to MCM5 at ...[more]

PMID: 32453425

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CryoEM structures of human CMG-ATPγS-DNA and CMG-AND-1 complexes.

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