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8EAH

SsoMCM hexamer bound to Mg/ADP-BeFx and 16-mer oligo-dT. Class 1

This is a non-PDB format compatible entry.
Summary for 8EAH
Entry DOI10.2210/pdb8eah/pdb
Related8EAF 8EAG 8EAI 8EAJ 8EAK 8EAL 8EAM
EMDB information27974 27975 27976 27977 27978 27979 27980 27981
DescriptorMinichromosome maintenance protein MCM, 16-mer oligo-dT, 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 weight419648.88
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 (2.48 Å)
Structure validation

227561

數據於2024-11-20公開中

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