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3DDX

HK97 bacteriophage capsid Expansion Intermediate-II model

Summary for 3DDX
Entry DOI10.2210/pdb3ddx/pdb
Related1OHG 2FTE 2GP1
DescriptorMajor capsid protein (1 entity in total)
Functional Keywordsbacteriophage, hk97, capsid protein, expansion intermediate, virion, icosahedral virus, virus
Biological sourceBacteriophage HK97
Total number of polymer chains7
Total formula weight215632.25
Authors
Lee, K.K.,Gan, L.,Conway, J.F.,Hendrix, R.W.,Steven, A.C.,Johnson, J.E. (deposition date: 2008-06-06, release date: 2008-11-04, Last modification date: 2025-03-05)
Primary citationLee, K.K.,Gan, L.,Tsuruta, H.,Moyer, C.,Conway, J.F.,Duda, R.L.,Hendrix, R.W.,Steven, A.C.,Johnson, J.E.
Virus capsid expansion driven by the capture of mobile surface loops.
Structure, 16:1491-1502, 2008
Cited by
PubMed Abstract: The capsids of tailed-DNA bacteriophages first assemble as procapsids, which mature by converting into a new form that is strong enough to contain a densely packed viral chromosome. We demonstrate that the intersubunit crosslinking that occurs during maturation of HK97 capsids actually promotes the structural transformation. Small-angle X-ray scattering and crosslinking assays reveal that a shift in the crosslink pattern accompanies conversion of a semimature particle, Expansion Intermediate-I/II, to a more mature state, Balloon. This transition occurs in a switch-like fashion. We find that crosslink formation shifts the global conformational balance to favor the balloon state. A pseudoatomic model of EI-I/II derived from cryo-EM provides insight into the relationship between crosslink formation and conformational switching.
PubMed: 18940605
DOI: 10.1016/j.str.2008.06.014
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (14 Å)
Structure validation

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