{"systematicName":"MCM2:MCM3:MCM4:MCM5:MCM6:MCM7","synonyms":["MCM2-7 complex","MCM2-7","Minichromosome maintenance (Mcm) 2-7"],"functions":["Essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells, associates with the origins of DNA replication to form part of the pre-replicative complex. Activation of the MCM complex at origins by cyclin-dependent kinases and the Cdc7 protein kinase leads to initiation of DNA synthesis. MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis."],"properties":["Forms a  ring-shaped, toroidal complex and use ATP binding and hydrolysis to engage DNA within its central channel. The isolated N-terminal domain of each subunit can drive assembly into a head-to-head double hexamer, Forms ATPase active sites at clefts between dimer interfaces, with one subunit contributing the P loop (a series of loops connecting adjacent parallel beta-strands), while the adjoining subunit contributes the lid, positioned C terminal to the P-loop domain. The P loop contains motifs involved in binding ATP (Walker A box) and orienting the nucleophilic water molecule (Walker B box), while the lid domain contains arginine finger motifs that contact the gamma-phosphate of ATP.\r\n\r\nTwo single hexameric complexes are loaded onto double-stranded origin DNA to form a double hexameric ing-shaped, toroidal complex which uses ATP binding and hydrolysis to engage DNA within its central channel.. The MCM2-MCM5 interaction appears to be the gate that promotes the opening of the MCM2–7 complex. The isolated N-terminal domain of each subunit drives assembly into a head-to-head double hexamer, Forms ATPase active sites at clefts between dimer interfaces, with one subunit contributing the P loop (a series of loops connecting adjacent parallel beta-strands), while the adjoining subunit contributes the lid, positioned C terminal to the P-loop domain. The P loop contains motifs involved in binding ATP (Walker A box) and orienting the nucleophilic water molecule (Walker B box), while the lid domain contains arginine finger motifs that contact the gamma-phosphate of ATP but only dimers of 7:3 and 4:7 appear to be active. 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