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8KFU

Crystal structure of ZmMOC1 in complex with a nicked Holliday junction soaked in Mn2+ for 180 seconds

Summary for 8KFU
Entry DOI10.2210/pdb8kfu/pdb
DescriptorHolliday junction resolvase MOC1, chloroplastic, DNA (33-MER), DNA (25-MER), ... (7 entities in total)
Functional Keywordsmoc1, holliday junction, time-resolved crystallography, hydrolase
Biological sourceZea mays
More
Total number of polymer chains5
Total formula weight55806.18
Authors
Zhang, D.,Luo, Z.,Lin, Z. (deposition date: 2023-08-16, release date: 2024-06-26, Last modification date: 2024-07-03)
Primary citationZhang, D.,Xu, S.,Luo, Z.,Lin, Z.
MOC1 cleaves Holliday junctions through a cooperative nick and counter-nick mechanism mediated by metal ions.
Nat Commun, 15:5140-5140, 2024
Cited by
PubMed Abstract: Holliday junction resolution is a crucial process in homologous recombination and DNA double-strand break repair. Complete Holliday junction resolution requires two stepwise incisions across the center of the junction, but the precise mechanism of metal ion-catalyzed Holliday junction cleavage remains elusive. Here, we perform a metal ion-triggered catalysis in crystals to investigate the mechanism of Holliday junction cleavage by MOC1. We capture the structures of MOC1 in complex with a nicked Holliday junction at various catalytic states, including the ground state, the one-metal ion binding state, and the two-metal ion binding state. Moreover, we also identify a third metal ion that may aid in the nucleophilic attack on the scissile phosphate. Further structural and biochemical analyses reveal a metal ion-mediated allosteric regulation between the two active sites, contributing to the enhancement of the second strand cleavage following the first strand cleavage, as well as the precise symmetric cleavage across the Holliday junction. Our work provides insights into the mechanism of metal ion-catalyzed Holliday junction resolution by MOC1, with implications for understanding how cells preserve genome integrity during the Holliday junction resolution phase.
PubMed: 38886375
DOI: 10.1038/s41467-024-49490-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

236963

건을2025-06-04부터공개중

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