4ME3

1.8 Angstrom Crystal Structure of the N-terminal Domain of an Archaeal MCM

Summary for 4ME3

• Entry DOI: 10.2210/pdb4me3/pdb
• Descriptor: DNA replication licensing factor MCM related protein, ZINC ION (3 entities in total)
• Functional Keywords: aaa+, zinc binding domain, helicase, replication
• Biological source: Thermoplasma acidophilum
• Total number of polymer chains: 1
• Total formula weight: 31518.89

Authors

Fu, Y.,Slaymaker, I.M.,Wang, G.,Chen, X.S. (deposition date: 2013-08-24, release date: 2014-01-08, Last modification date: 2024-02-28)

Primary citation

Fu, Y.,Slaymaker, I.M.,Wang, J.,Wang, G.,Chen, X.S.
The 1.8- angstrom Crystal Structure of the N-Terminal Domain of an Archaeal MCM as a Right-Handed Filament.
J.Mol.Biol., 426:1512-1523, 2014

PubMed Abstract: Mini-chromosome maintenance (MCM) proteins are the replicative helicase necessary for DNA replication in both eukarya and archaea. Most of archaea only have one MCM gene. Here, we report a 1.8-Å crystal structure of the N-terminal MCM from the archaeon Thermoplasma acidophilum (tapMCM). In the structure, the MCM N-terminus forms a right-handed filament that contains six subunits in each turn, with a diameter of 25Å of the central channel opening. The inner surface is highly positively charged, indicating DNA binding. This filament structure with six subunits per turn may also suggests a potential role for an open-ring structure for hexameric MCM and dynamic conformational changes in initiation and elongation stages of DNA replication.

PubMed: 24378617
DOI: 10.1016/j.jmb.2013.12.025

Experimental method

X-RAY DIFFRACTION (1.794 Å)