The maturation-dependent conformational change of the major capsid protein of bacteriophage T4 involves a substantial change in secondary structure

Biochemistry ◽  
1990 ◽  
Vol 29 (23) ◽  
pp. 5556-5561 ◽  
Author(s):  
Alasdair C. Steven ◽  
Heather Greenstone ◽  
Adelia C. Bauer ◽  
Robert W. Williams
Keyword(s):  
Secondary Structure ◽  
Conformational Change ◽  
Capsid Protein ◽  
Major Capsid Protein ◽  
Bacteriophage T4 ◽  
Substantial Change

scholarly journals Cryo-EM structure of the bacteriophage T4 isometric head at 3.3-Å resolution and its relevance to the assembly of icosahedral viruses

2017 ◽  
Vol 114 (39) ◽  
pp. E8184-E8193 ◽  
Author(s):  
Zhenguo Chen ◽  
Lei Sun ◽  
Zhihong Zhang ◽  
Andrei Fokine ◽  
Victor Padilla-Sanchez ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Bacteriophage T4 ◽  
Hexagonal Lattice ◽  
Scaffolding Proteins ◽  
Outer Capsid Protein ◽  
Head Assembly ◽  
Icosahedral Viruses ◽  
End Caps ◽  
Outer Capsid

The 3.3-Å cryo-EM structure of the 860-Å-diameter isometric mutant bacteriophage T4 capsid has been determined. WT T4 has a prolate capsid characterized by triangulation numbers (T numbers) Tend= 13 for end caps and Tmid= 20 for midsection. A mutation in the major capsid protein, gp23, produced T=13 icosahedral capsids. The capsid is stabilized by 660 copies of the outer capsid protein, Soc, which clamp adjacent gp23 hexamers. The occupancies of Soc molecules are proportional to the size of the angle between the planes of adjacent hexameric capsomers. The angle between adjacent hexameric capsomers is greatest around the fivefold vertices, where there is the largest deviation from a planar hexagonal array. Thus, the Soc molecules reinforce the structure where there is the greatest strain in the gp23 hexagonal lattice. Mutations that change the angles between adjacent capsomers affect the positions of the pentameric vertices, resulting in different triangulation numbers in bacteriophage T4. The analysis of the T4 mutant head assembly gives guidance to how other icosahedral viruses reproducibly assemble into capsids with a predetermined T number, although the influence of scaffolding proteins is also important.

scholarly journals Unravelling the chaperonin‐assisted folding of the bacteriophage T4 major capsid protein

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Stephane Calmat ◽  
Harm Heerikhuizen ◽  
Christoph F. Schmidt ◽  
Erwin J.G. Peterman ◽  
Saskia M. Vies
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Bacteriophage T4

scholarly journals Identification of a nonconventional motif necessary for the nuclear import of the human parvovirus B19 major capsid protein (VP2)

Virology ◽  
2003 ◽  
Vol 306 (1) ◽  
pp. 25-32 ◽  
Author(s):  
Sylvie Pillet ◽  
Zeinab Annan ◽  
Serge Fichelson ◽  
F.rédéric Morinet
Keyword(s):  
Capsid Protein ◽  
Nuclear Import ◽  
Major Capsid Protein ◽  
Parvovirus B19 ◽  
Human Parvovirus B19
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