Cargando…
A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex
Tailed bacteriophages and herpesviruses use a transient scaffold to assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold portal is thought to nucleate the assembly. How does the scaffold orchestrate this step? We have deter...
Autores principales: | Huet, Alexis, Oh, Bonnie, Maurer, Josh, Duda, Robert L., Conway, James F. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10275583/ https://www.ncbi.nlm.nih.gov/pubmed/37327331 http://dx.doi.org/10.1126/sciadv.adg8868 |
Ejemplares similares
-
Capsids and Genomes of Jumbo-Sized Bacteriophages Reveal the Evolutionary Reach of the HK97 Fold
por: Hua, Jianfei, et al.
Publicado: (2017) -
The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy
por: Newcomer, Rebecca L, et al.
Publicado: (2019) -
A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 Å resolution
por: Zhang, Xing, et al.
Publicado: (2013) -
Correction: A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 Å resolution
por: Zhang, Xing, et al.
Publicado: (2015) -
Insights into a viral motor: the structure of the HK97 packaging termination assembly
por: Hawkins, Dorothy E D P, et al.
Publicado: (2023)