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TitleStructural study of the N-terminal domain of human MCM8/9 complex.
Journal, issue, pagesStructure, Vol. 29, Issue 10, Page 1171-11181.e4, Year 2021
Publish dateOct 7, 2021
AuthorsJun Li / Daqi Yu / Lan Liu / Huanhuan Liang / Qi Ouyang / Yingfang Liu /
PubMed AbstractMCM8/9 is a complex involved in homologous recombination (HR) repair pathway. MCM8/9 dysfunction can cause genome instability and result in primary ovarian insufficiency (POI). However, the mechanism ...MCM8/9 is a complex involved in homologous recombination (HR) repair pathway. MCM8/9 dysfunction can cause genome instability and result in primary ovarian insufficiency (POI). However, the mechanism underlying these effects is largely unknown. Here, we report crystal structures of the N-terminal domains (NTDs) of MCM8 and MCM9, and build a ring-shaped NTD structure based on a 6.6 Å resolution cryoelectron microscopy map. This shows that the MCM8/9 complex forms a 3:3 heterohexamer in an alternating pattern. A positively charged DNA binding channel and a putative ssDNA exit pathway for fork DNA unwinding are revealed. Based on the atomic model, the potential effects of the clinical POI mutants are interpreted. Surprisingly, the zinc-finger motifs are found to be capable of binding an iron atom as well. Overall, our results provide a model for the formation of the MCM8/9 complex and provide a path for further studies.
External linksStructure / PubMed:34043945
MethodsEM (single particle) / X-ray diffraction
Resolution2.55 - 7.1 Å
Structure data

EMDB-0823:
Cryo-EM map of human MCM8/9 complex
Method: EM (single particle) / Resolution: 7.1 Å

EMDB-0824:
Cryo-EM map for N terminal domain of human MCM8/9 complex
Method: EM (single particle) / Resolution: 6.6 Å

PDB-7dp3:
Human MCM8 N-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-7dpd:
Human MCM9 N-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / Zinc Finger / DNA binding

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