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

Wen Jiang; Zongli Li; Zhixian Zhang; Matthew L. Baker; Peter E. Prevelige; Wah Chiu

doi:10.1038/nsb891

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

Wen Jiang, Zongli Li, Zhixian Zhang, Matthew L. Baker, Peter E. Prevelige, Wah Chiu

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181 Scopus citations

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 A and 9.5 A 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.

Original language	English (US)
Pages (from-to)	131-135
Number of pages	5
Journal	Nature Structural Biology
Volume	10
Issue number	2
DOIs	https://doi.org/10.1038/nsb891
State	Published - Feb 1 2003

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Genetics

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10.1038/nsb891

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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 A and 9.5 A 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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AU - Li, Zongli

AU - Zhang, Zhixian

AU - Baker, Matthew L.

AU - Prevelige, Peter E.

AU - Chiu, Wah

PY - 2003/2/1

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

Abstract

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