Summary for 5V8F
| Entry DOI | 10.2210/pdb5v8f/pdb |
| EMDB information | 8540 |
| Descriptor | DNA replication licensing factor MCM2, Origin recognition complex subunit 2, Origin recognition complex subunit 3, ... (17 entities in total) |
| Functional Keywords | dna replication, cryo-em, occm, replication |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 16 |
| Total formula weight | 1170843.94 |
| Authors | Yuan, Z.,Riera, A.,Bai, L.,Sun, J.,Spanos, C.,Chen, Z.A.,Barbon, M.,Rappsilber, J.,Stillman, B.,Speck, C.,Li, H. (deposition date: 2017-03-21, release date: 2017-05-10, Last modification date: 2024-10-09) |
| Primary citation | Yuan, Z.,Riera, A.,Bai, L.,Sun, J.,Nandi, S.,Spanos, C.,Chen, Z.A.,Barbon, M.,Rappsilber, J.,Stillman, B.,Speck, C.,Li, H. Structural basis of Mcm2-7 replicative helicase loading by ORC-Cdc6 and Cdt1. Nat. Struct. Mol. Biol., 24:316-324, 2017 Cited by PubMed Abstract: To initiate DNA replication, the origin recognition complex (ORC) and Cdc6 load an Mcm2-7 double hexamer onto DNA. Without ATP hydrolysis, ORC-Cdc6 recruits one Cdt1-bound Mcm2-7 hexamer, thus forming an ORC-Cdc6-Cdt1-Mcm2-7 (OCCM) helicase-loading intermediate. Here we report a 3.9-Å structure of Saccharomyces cerevisiae OCCM on DNA. Flexible Mcm2-7 winged-helix domains (WHDs) engage ORC-Cdc6. A three-domain Cdt1 configuration embraces Mcm2, Mcm4, and Mcm6, thus comprising nearly half of the hexamer. The Cdt1 C-terminal domain extends to the Mcm6 WHD, which binds the Orc4 WHD. DNA passes through the ORC-Cdc6 and Mcm2-7 rings. Origin DNA interaction is mediated by an α-helix within Orc4 and positively charged loops within Orc2 and Cdc6. The Mcm2-7 C-tier AAA+ ring is topologically closed by an Mcm5 loop that embraces Mcm2, but the N-tier-ring Mcm2-Mcm5 interface remains open. This structure suggests a loading mechanism of the first Cdt1-bound Mcm2-7 hexamer by ORC-Cdc6. PubMed: 28191893DOI: 10.1038/nsmb.3372 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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