Cargando…
Cryo-EM structure of Mcm2-7 double hexamer on DNA suggests a lagging-strand DNA extrusion model
During replication initiation, the core component of the helicase—the Mcm2-7 hexamer—is loaded on origin DNA as a double hexamer (DH). The two ring-shaped hexamers are staggered, leading to a kinked axial channel. How the origin DNA interacts with the axial channel is not understood, but the interac...
Autores principales: | Noguchi, Yasunori, Yuan, Zuanning, Bai, Lin, Schneider, Sarah, Zhao, Gongpu, Stillman, Bruce, Speck, Christian, Li, Huilin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5692578/ https://www.ncbi.nlm.nih.gov/pubmed/29078375 http://dx.doi.org/10.1073/pnas.1712537114 |
Ejemplares similares
-
Structural and mechanistic insights into Mcm2–7 double-hexamer assembly and function
por: Sun, Jingchuan, et al.
Publicado: (2014) -
An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity
por: Jin, Mingliang, et al.
Publicado: (2019) -
Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans
por: Yang, Tzu-Jing, et al.
Publicado: (2020) -
Mechanism of head-to-head MCM double-hexamer formation revealed by cryo-EM
por: Miller, Thomas CR, et al.
Publicado: (2019) -
ATP hydrolysis-coupled peptide translocation mechanism of Mycobacterium tuberculosis ClpB
por: Yu, Hongjun, et al.
Publicado: (2018)