5IY0
PfMCM N-terminal domain double hexamer
Summary for 5IY0
| Entry DOI | 10.2210/pdb5iy0/pdb |
| Descriptor | Cell division control protein 21, ZINC ION (2 entities in total) |
| Functional Keywords | replication, dna binding protein, replication dna binding protein |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 6 |
| Total formula weight | 176796.72 |
| Authors | Meagher, M.,Enemark, E.J. (deposition date: 2016-03-23, release date: 2016-07-13, Last modification date: 2023-09-27) |
| Primary citation | Meagher, M.,Enemark, E.J. Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N-terminal domain. Acta Crystallogr.,Sect.F, 72:545-551, 2016 Cited by PubMed Abstract: The crystal structure of the N-terminal domain of the Pyrococcus furiosus minichromosome maintenance (MCM) protein as a double hexamer is described. The MCM complex is a ring-shaped helicase that unwinds DNA at the replication fork of eukaryotes and archaea. Prior to replication initiation, the MCM complex assembles as an inactive double hexamer at specific sites of DNA. The presented structure is highly consistent with previous MCM double-hexamer structures and shows two MCM hexamers with a head-to-head interaction mediated by the N-terminal domain. Minor differences include a diminished head-to-head interaction and a slightly reduced inter-hexamer rotation. PubMed: 27380371DOI: 10.1107/S2053230X1600858X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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