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8EAM

SsoMCM hexamer bound to Mg/ADP-BeFx and DNA. Class 2. Merged particles from datasets with 3 different DNA entities

This is a non-PDB format compatible entry.
Summary for 8EAM
Entry DOI10.2210/pdb8eam/pdb
Related8EAF 8EAG 8EAH 8EAI 8EAJ 8EAK 8EAL
EMDB information27974 27975 27976 27977 27978 27979 27980 27981
DescriptorMinichromosome maintenance protein MCM, DNA, ZINC ION, ... (6 entities in total)
Functional Keywordshelicase, atpase, replication, transferase-dna complex, transferase/dna
Biological sourceSaccharolobus solfataricus P2
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Total number of polymer chains7
Total formula weight417915.60
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 citationMeagher, 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: 36499022
DOI: 10.3390/ijms232314678
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.59 Å)
Structure validation

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