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New page: left|200px<br /><applet load="1za7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1za7, resolution 2.70Å" /> '''The crystal structur...
 
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[[Image:1za7.gif|left|200px]]<br /><applet load="1za7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1za7, resolution 2.70&Aring;" />
'''The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.'''<br />


==Overview==
==The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.==
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.
<StructureSection load='1za7' size='340' side='right'caption='[[1za7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1za7]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZA7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1za7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1za7 OCA], [https://pdbe.org/1za7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1za7 RCSB], [https://www.ebi.ac.uk/pdbsum/1za7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1za7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_CCMV CAPSD_CCMV] Capsid protein. Probably binds RNA and plays a role in packaging.<ref>PMID:15731222</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 Structure==
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<ref>PMID:16537626</ref>
1ZA7 is a [http://en.wikipedia.org/wiki/Single_protein 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZA7 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16537626 16537626]
</div>
<div class="pdbe-citations 1za7" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cowpea Chlorotic Mottle Virus|Cowpea Chlorotic Mottle Virus]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cowpea chlorotic mottle virus]]
[[Category: Cowpea chlorotic mottle virus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bothner, B.]]
[[Category: Bothner B]]
[[Category: Johnson, J.E.]]
[[Category: Johnson JE]]
[[Category: Qu, C.]]
[[Category: Qu C]]
[[Category: Speir, J.A.]]
[[Category: Speir JA]]
[[Category: Willits, D.A.]]
[[Category: Willits DA]]
[[Category: Young, M.J.]]
[[Category: Young MJ]]
[[Category: beta barrel]]
[[Category: beta hexamer]]
[[Category: bromovirus]]
[[Category: icosahedral particle]]
[[Category: icosahedral virus]]
[[Category: mutant virus capsid structure]]
[[Category: point mutation]]
[[Category: stable mutant]]
[[Category: stablizing mutation]]
 
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Retrieved from "https://proteopedia.org/1za7"