8OUW
Cryo-EM structure of CMG helicase bound to TIM-1/TIPN-1 and homodimeric DNSN-1 on fork DNA (Caenorhabditis elegans)
This is a non-PDB format compatible entry.
Summary for 8OUW
| Entry DOI | 10.2210/pdb8ouw/pdb |
| EMDB information | 17204 |
| Descriptor | DNA replication licensing factor MCM2, DNA replication complex GINS protein SLD5, Cell division control protein 45 homolog, ... (19 entities in total) |
| Functional Keywords | dna replication, dna replication initiation, replisome, donson, replication |
| Biological source | Caenorhabditis elegans More |
| Total number of polymer chains | 19 |
| Total formula weight | 1153734.08 |
| Authors | Jenkyn-Bedford, M.,Yeeles, J.T.P.,Labib, K.P.M. (deposition date: 2023-04-25, release date: 2023-08-16, Last modification date: 2023-10-04) |
| Primary citation | Xia, Y.,Sonneville, R.,Jenkyn-Bedford, M.,Ji, L.,Alabert, C.,Hong, Y.,Yeeles, J.T.P.,Labib, K.P.M. DNSN-1 recruits GINS for CMG helicase assembly during DNA replication initiation in Caenorhabditis elegans. Science, 381:eadi4932-eadi4932, 2023 Cited by PubMed Abstract: Assembly of the CMG (CDC-45-MCM-2-7-GINS) helicase is the key regulated step during eukaryotic DNA replication initiation. Until now, it was unclear whether metazoa require additional factors that are not present in yeast. In this work, we show that DNSN-1, the ortholog of human DONSON, functions during helicase assembly in a complex with MUS-101/TOPBP1. DNSN-1 is required to recruit the GINS complex to chromatin, and a cryo-electron microscopy structure indicates that DNSN-1 positions GINS on the MCM-2-7 helicase motor (comprising the six MCM-2 to MCM-7 proteins), by direct binding of DNSN-1 to GINS and MCM-3, using interfaces that we show are important for initiation and essential for viability. These findings identify DNSN-1 as a missing link in our understanding of DNA replication initiation, suggesting that initiation defects underlie the human disease syndrome that results from DONSON mutations. PubMed: 37590372DOI: 10.1126/science.adi4932 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.75 Å) |
Structure validation
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