4POF

PfMCM N-terminal domain without DNA

Summary for 4POF

• Entry DOI: 10.2210/pdb4pof/pdb
• Related: 4POG
• Descriptor: Cell division control protein 21, ZINC ION (2 entities in total)
• Functional Keywords: ob-fold, dna replication, replication, dna binding protein
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 6
• Total formula weight: 176796.72

Authors

Froelich, C.A.,Kang, S.,Epling, L.B.,Bell, S.P.,Enemark, E.J. (deposition date: 2014-02-25, release date: 2014-04-09, Last modification date: 2023-09-20)

Primary citation

Froelich, C.A.,Kang, S.,Epling, L.B.,Bell, S.P.,Enemark, E.J.
A conserved MCM single-stranded DNA binding element is essential for replication initiation.
Elife, 3:e01993-e01993, 2014

PubMed Abstract: The ring-shaped MCM helicase is essential to all phases of DNA replication. The complex loads at replication origins as an inactive double-hexamer encircling duplex DNA. Helicase activation converts this species to two active single hexamers that encircle single-stranded DNA (ssDNA). The molecular details of MCM DNA interactions during these events are unknown. We determined the crystal structure of the Pyrococcus furiosus MCM N-terminal domain hexamer bound to ssDNA and define a conserved MCM-ssDNA binding motif (MSSB). Intriguingly, ssDNA binds the MCM ring interior perpendicular to the central channel with defined polarity. In eukaryotes, the MSSB is conserved in several Mcm2-7 subunits, and MSSB mutant combinations in S. cerevisiae Mcm2-7 are not viable. Mutant Mcm2-7 complexes assemble and are recruited to replication origins, but are defective in helicase loading and activation. Our findings identify an important MCM-ssDNA interaction and suggest it functions during helicase activation to select the strand for translocation. DOI: http://dx.doi.org/10.7554/eLife.01993.001.

PubMed: 24692448
DOI: 10.7554/eLife.01993

Experimental method

X-RAY DIFFRACTION (2.648 Å)