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- Title
Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions.
- Authors
Jiang, Wen; Li, Zongli; Zhang, Zhixian; Baker, Matthew L.; Prevelige, Peter E.; Chiu, Wah
- Abstract
Bacteriophage P22 is a prototypical biological machine used for studying protein complex assembly and capsid maturation. Using cryo-EM, we solved the structures of P22 before and after the capsid maturation at 8.5 Å and 9.5 Å resolutions, respectively. These structures allowed visualization of α-helices and β-sheets from which the capsid protein fold is derived. The capsid fold is similar to that of the coat protein of HK97 bacteriophage. The cryo-EM shows that a large conformational change of the P22 capsid during maturation transition involves not only the domain movement of individual subunits, but also refolding of the capsid protein.
- Subjects
BACTERIOPHAGES; PROTEIN folding; DNA; BIOCHEMISTRY
- Publication
Nature Structural Biology, 2003, Vol 10, Issue 2, p131
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/nsb891