8EAG
SsoMCM hexamer bound to Mg/ADP-BeFx and 12-mer oligo-dT. Class 2
This is a non-PDB format compatible entry.
Summary for 8EAG
| Entry DOI | 10.2210/pdb8eag/pdb |
| Related | 8EAF 8EAH 8EAI 8EAJ 8EAK 8EAL 8EAM |
| EMDB information | 27975 27976 27978 27979 27980 27981 |
| Descriptor | Minichromosome maintenance protein MCM, 12-mer oligo-dT, ZINC ION, ... (6 entities in total) |
| Functional Keywords | helicase, atpase, replication, transferase-dna complex, transferase/dna |
| Biological source | Saccharolobus solfataricus P2 More |
| Total number of polymer chains | 7 |
| Total formula weight | 417915.60 |
| Authors | Meagher, M.,Myasnikov, A.,Enemark, E.J. (deposition date: 2022-08-29, release date: 2022-12-14, Last modification date: 2024-06-19) |
| Primary citation | Meagher, M.,Myasnikov, A.,Enemark, E.J. Two Distinct Modes of DNA Binding by an MCM Helicase Enable DNA Translocation. Int J Mol Sci, 23:-, 2022 Cited by PubMed Abstract: A six-subunit ATPase ring forms the central hub of the replication forks in all domains of life. This ring performs a helicase function to separate the two complementary DNA strands to be replicated and drives the replication machinery along the DNA. Disruption of this helicase/ATPase ring is associated with genetic instability and diseases such as cancer. The helicase/ATPase rings of eukaryotes and archaea consist of six minichromosome maintenance (MCM) proteins. Prior structural studies have shown that MCM rings bind one encircled strand of DNA in a spiral staircase, suggesting that the ring pulls this strand of DNA through its central pore in a hand-over-hand mechanism where the subunit at the bottom of the staircase dissociates from DNA and re-binds DNA one step above the staircase. With high-resolution cryo-EM, we show that the MCM ring of the archaeal organism binds an encircled DNA strand in two different modes with different numbers of subunits engaged to DNA, illustrating a plausible mechanism for the alternating steps of DNA dissociation and re-association that occur during DNA translocation. PubMed: 36499022DOI: 10.3390/ijms232314678 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.01 Å) |
Structure validation
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