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Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions

Nature Structural Biology volume 10, pages 131–135 (2003)Cite this article

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.

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Figure 1: Structure determination of P22.
Figure 2: Identification of secondary structures.
Figure 3: Structural comparison with HK97.
Figure 4: Stereo view of the molecular contacts of adjacent subunits in hexamer of the P22

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Acknowledgements

We thank J. King and B. Green of MIT for providing the phage sample for an earlier investigation. This research has been supported by grants from National Institute of Allergy and Infectious Diseases, National Center for Research Resources, National Institute of General Medical Science, the National Library of Medicine training grant and the Agouron Institute.

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Authors and Affiliations

  1. Verna and Marrs McLean Department of Biochemistry and Molecular Biology, National Center for Macromolecular Imaging, Baylor College of Medicine, One Baylor Plaza, Houston, 77030, Texas, USA

    Wen Jiang, Zongli Li, Zhixian Zhang, Matthew L. Baker & Wah Chiu

  2. Department of Microbiology, University of Alabama at Birmingham, Birmingham, 35294, Alabama, USA

    Peter E. Prevelige Jr.

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  1. Wen Jiang
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Correspondence to Wah Chiu.

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Jiang, W., Li, Z., Zhang, Z. et al. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Mol Biol 10, 131–135 (2003). https://doi.org/10.1038/nsb891

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