|Title||CryoEM structures of human CMG-ATPγS-DNA and CMG-AND-1 complexes.|
|Journal, issue, pages||Nucleic Acids Res, Vol. 48, Issue 12, Page 6980-6995, Year 2020|
|Publish date||Jul 9, 2020|
|Authors||Neil J Rzechorzek / Steven W Hardwick / Vincentius A Jatikusumo / Dimitri Y Chirgadze / Luca Pellegrini /|
|PubMed Abstract||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 ...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 the 3'-end of the DNA spiral, but only MCM6, 4, 7 and 3 make a full set of interactions. DNA binding correlates with nucleotide occupancy: five MCM subunits are bound to either ATPγS or ADP, whereas the apo MCM2-5 interface remains open. We further report the cryoEM structure of human CMG bound to the replisome hub AND-1 (CMGA). The AND-1 trimer uses one β-propeller domain of its trimerisation region to dock onto the side of the helicase assembly formed by Cdc45 and GINS. In the resulting CMGA architecture, the AND-1 trimer is closely positioned to the fork DNA while its CIP (Ctf4-interacting peptide)-binding helical domains remain available to recruit partner proteins.|
|External links||Nucleic Acids Res / PubMed:32453425 / PubMed Central|
|Methods||EM (single particle)|
|Resolution||3.29 - 6.77 Å|
|Keywords||Adenosine Triphosphatases / Adenosine Triphosphate / CDC45 protein, human / Cell Cycle Proteins / Cryoelectron Microscopy / Crystallography, X-Ray / DNA / DNA Helicases / DNA Replication / DNA-Binding Proteins / Humans / Minichromosome Maintenance Proteins / Models, Molecular / Multiprotein Complexes / Nucleic Acid Conformation / Protein Conformation / WDHD1 protein, human / adenosine 5'-O-(3-thiotriphosphate) / REPLICATION / CMG / Helicase / ATPase / Replisome|
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