1za7: Difference between revisions
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[[Image:1za7.gif|left|200px]] | [[Image:1za7.gif|left|200px]] | ||
'''The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.''' | {{Structure | ||
|PDB= 1za7 |SIZE=350|CAPTION= <scene name='initialview01'>1za7</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= RNA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12303 Cowpea chlorotic mottle virus]) | |||
}} | |||
'''The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZA7 is a [ | 1ZA7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cowpea_chlorotic_mottle_virus Cowpea chlorotic mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZA7 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16537626 16537626] | ||
[[Category: Cowpea chlorotic mottle virus]] | [[Category: Cowpea chlorotic mottle virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: stablizing mutation]] | [[Category: stablizing mutation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:33:02 2008'' | ||
Revision as of 16:33, 20 March 2008
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| , resolution 2.70Å | |||||||
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| Gene: | RNA4 (Cowpea chlorotic mottle virus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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