1za7: Difference between revisions
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'''The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.''' | '''The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.''' | ||
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[[Category: Willits, D A.]] | [[Category: Willits, D A.]] | ||
[[Category: Young, M J.]] | [[Category: Young, M J.]] | ||
[[Category: | [[Category: Beta barrel]] | ||
[[Category: | [[Category: Beta hexamer]] | ||
[[Category: | [[Category: Bromovirus]] | ||
[[Category: | [[Category: Icosahedral particle]] | ||
[[Category: | [[Category: Icosahedral virus]] | ||
[[Category: | [[Category: Mutant virus capsid structure]] | ||
[[Category: | [[Category: Point mutation]] | ||
[[Category: | [[Category: Stable mutant]] | ||
[[Category: | [[Category: Stablizing mutation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:22:45 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:22, 3 May 2008
The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.
OverviewOverview
Structural transitions in viral capsids play a critical role in the virus life cycle, including assembly, disassembly, and release of the packaged nucleic acid. Cowpea chlorotic mottle virus (CCMV) undergoes a well-studied reversible structural expansion in vitro in which the capsid expands by 10%. The swollen form of the particle can be completely disassembled by increasing the salt concentration to 1 M. Remarkably, a single-residue mutant of the CCMV N-terminal arm, K42R, is not susceptible to dissociation in high salt (salt-stable CCMV [SS-CCMV]) and retains 70% of wild-type infectivity. We present the combined structural and biophysical basis for the chemical stability and viability of the SS-CCMV particles. A 2.7-A resolution crystal structure of the SS-CCMV capsid shows an addition of 660 new intersubunit interactions per particle at the center of the 20 hexameric capsomeres, which are a direct result of the K42R mutation. Protease-based mapping experiments of intact particles demonstrate that both the swollen and closed forms of the wild-type and SS-CCMV particles have highly dynamic N-terminal regions, yet the SS-CCMV particles are more resistant to degradation. Thus, the increase in SS-CCMV particle stability is a result of concentrated tethering of subunits at a local symmetry interface (i.e., quasi-sixfold axes) that does not interfere with the function of other key symmetry interfaces (i.e., fivefold, twofold, quasi-threefold axes). The result is a particle that is still dynamic but insensitive to high salt due to a new series of bonds that are resistant to high ionic strength and preserve the overall particle structure.
About this StructureAbout this Structure
1ZA7 is a Single protein structure of sequence from Cowpea chlorotic mottle virus. Full crystallographic information is available from OCA.
ReferenceReference
Enhanced local symmetry interactions globally stabilize a mutant virus capsid that maintains infectivity and capsid dynamics., Speir JA, Bothner B, Qu C, Willits DA, Young MJ, Johnson JE, J Virol. 2006 Apr;80(7):3582-91. PMID:16537626 Page seeded by OCA on Sat May 3 17:22:45 2008