Nature Structural Biology10, 131 - 135 (2003)
Published online: 21 January 2003; | doi:10.1038/nsb891
Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
Wen Jiang1, Zongli Li1, Zhixian Zhang1, Matthew L. Baker1, Peter E. Prevelige Jr.2
& Wah Chiu1
1
National Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
2
Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
Correspondence should be addressed to Wah Chiu wah@bcm.tmc.edu
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 -helices and -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.
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-helices and 
-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.
