1za7: Difference between revisions

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{{Seed}}
[[Image:1za7.png|left|200px]]


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==The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.==
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<StructureSection load='1za7' size='340' side='right'caption='[[1za7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
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</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>
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<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>
{{STRUCTURE_1za7|  PDB=1za7  |  SCENE=  }}
</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.


===The crystal structure of salt stable cowpea cholorotic mottle virus at 2.7 angstroms resolution.===
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1za7" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_16537626}}, adds the Publication Abstract to the page
*[[Cowpea Chlorotic Mottle Virus|Cowpea Chlorotic Mottle Virus]]
(as it appears on PubMed at http://www.pubmed.gov), where 16537626 is the PubMed ID number.
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
{{ABSTRACT_PUBMED_16537626}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
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==
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]
 
Analysis of a salt stable mutant of cowpea chlorotic mottle virus., Fox JM, Zhao X, Speir JA, Young MJ, Virology. 1996 Aug 1;222(1):115-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8806492 8806492]
 
Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy., Speir JA, Munshi S, Wang G, Baker TS, Johnson JE, Structure. 1995 Jan 15;3(1):63-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7743132 7743132]
[[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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