This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1za7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE= RNA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12303 Cowpea chlorotic mottle virus])
|GENE= RNA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12303 Cowpea chlorotic mottle virus])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1cwp|1cwp]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1za7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1za7 OCA], [http://www.ebi.ac.uk/pdbsum/1za7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1za7 RCSB]</span>
}}
}}
Line 38: Line 41:
[[Category: stablizing mutation]]
[[Category: stablizing mutation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:33:02 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:33:04 2008''

Revision as of 22:33, 30 March 2008

Image:1za7.gif


PDB ID 1za7

Drag the structure with the mouse to rotate
, resolution 2.70Å
Gene: RNA4 (Cowpea chlorotic mottle virus)
Related: 1cwp


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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

1ZA7 is a Single protein structure of sequence from Cowpea chlorotic mottle virus. Full crystallographic information is available from 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:16537626

Page seeded by OCA on Mon Mar 31 01:33:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1za7"
Personal tools