Structural highlights
Function
MCM2_XENLA Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.[1] [2] [3]
References
- ↑ Ying CY, Gautier J. The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding. EMBO J. 2005 Dec 21;24(24):4334-44. PMID:16369567 doi:10.1038/sj.emboj.7600892
- ↑ Thömmes P, Kubota Y, Takisawa H, Blow JJ. The RLF-M component of the replication licensing system forms complexes containing all six MCM/P1 polypeptides. EMBO J. 1997 Jun 2;16(11):3312-9. PMID:9214646 doi:10.1093/emboj/16.11.3312
- ↑ Kubota Y, Mimura S, Nishimoto S, Masuda T, Nojima H, Takisawa H. Licensing of DNA replication by a multi-protein complex of MCM/P1 proteins in Xenopus eggs. EMBO J. 1997 Jun 2;16(11):3320-31. PMID:9214647 doi:10.1093/emboj/16.11.3320
