Summary for 7PFO
| Entry DOI | 10.2210/pdb7pfo/pdb |
| EMDB information | 13375 13376 13377 13384 13457 |
| Descriptor | DNA replication licensing factor MCM2, DNA replication complex GINS protein PSF1, DNA replication complex GINS protein PSF2, ... (23 entities in total) |
| Functional Keywords | dna replication, helicase, cmg, timeless, tipin, claspin, and-1, epsilon, polymerase, replisome, replication |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 21 |
| Total formula weight | 1797086.04 |
| Authors | Jones, M.J.,Yeeles, J.T.P. (deposition date: 2021-08-11, release date: 2021-11-10, Last modification date: 2023-10-18) |
| Primary citation | Jones, M.L.,Baris, Y.,Taylor, M.R.G.,Yeeles, J.T.P. Structure of a human replisome shows the organisation and interactions of a DNA replication machine. Embo J., 40:e108819-e108819, 2021 Cited by PubMed Abstract: The human replisome is an elaborate arrangement of molecular machines responsible for accurate chromosome replication. At its heart is the CDC45-MCM-GINS (CMG) helicase, which, in addition to unwinding the parental DNA duplex, arranges many proteins including the leading-strand polymerase Pol ε, together with TIMELESS-TIPIN, CLASPIN and AND-1 that have key and varied roles in maintaining smooth replisome progression. How these proteins are coordinated in the human replisome is poorly understood. We have determined a 3.2 Å cryo-EM structure of a human replisome comprising CMG, Pol ε, TIMELESS-TIPIN, CLASPIN and AND-1 bound to replication fork DNA. The structure permits a detailed understanding of how AND-1, TIMELESS-TIPIN and Pol ε engage CMG, reveals how CLASPIN binds to multiple replisome components and identifies the position of the Pol ε catalytic domain. Furthermore, the intricate network of contacts contributed by MCM subunits and TIMELESS-TIPIN with replication fork DNA suggests a mechanism for strand separation. PubMed: 34694004DOI: 10.15252/embj.2021108819 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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