Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions.
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 A and 9.5 A resolutions, respectively. These structures allowed visualization of alpha-helices and beta-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.
Jiang
Wen
W
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.
Li
Zongli
Z
Zhang
Zhixian
Z
Baker
Matthew L
ML
Prevelige
Peter E
PE
Chiu
Wah
W
D017100:Bacteriophage P22 / Q000737:chemistry* / Q000254:growth & development / Q000648:ultrastructure*; D036022:Capsid Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D021122:Protein Subunits
D036022:Capsid Proteins; D021122:Protein Subunits