2izw

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[[Image:2izw.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2izw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izw OCA], [http://www.ebi.ac.uk/pdbsum/2izw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2izw RCSB]</span>
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'''CRYSTAL STRUCTURE OF RYEGRASS MOTTLE VIRUS'''
'''CRYSTAL STRUCTURE OF RYEGRASS MOTTLE VIRUS'''
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[[Category: Truve, E.]]
[[Category: Truve, E.]]
[[Category: Zeltins, A.]]
[[Category: Zeltins, A.]]
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[[Category: assembly]]
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[[Category: Assembly]]
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[[Category: capsid protein]]
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[[Category: Capsid protein]]
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[[Category: rna]]
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[[Category: Rna]]
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[[Category: virus]]
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[[Category: Virus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:08:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:51:07 2008''
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Revision as of 05:08, 4 May 2008

Template:STRUCTURE 2izw

CRYSTAL STRUCTURE OF RYEGRASS MOTTLE VIRUS


Overview

The crystal structure of the sobemovirus Ryegrass mottle virus (RGMoV) has been determined at 2.9 A resolution. The coat protein has a canonical jellyroll beta-sandwich fold. In comparison to other sobemoviruses the RGMoV coat protein is missing several residues in two of the loop regions. The first loop contributes to contacts between subunits around the quasi-threefold symmetry axis. The altered contact interface results in tilting of the subunits towards the quasi-threefold axis. The assembly of the T=3 capsid of sobemoviruses is controlled by the N-termini of C subunits forming a so-called beta-annulus. The other loop that is smaller in the RGMoV structure contains a helix that participates in stabilization of the beta-annulus in other sobemoviruses. The loss of interaction between the RGMoV loop and the beta-annulus has been compensated for by additional interactions between the N-terminal arms. As a consequence of these differences, the diameter of the RGMoV particle is 8 A smaller than that of the other sobemoviruses. The interactions of coat proteins in sobemovirus capsids involve calcium ions. Depletion of calcium ions results in particle swelling, which is considered a first step in disassembly. We could not identify any density for metal ions in the proximity of the conserved residues normally involved in calcium binding, but the RGMoV structure does not show any signs of swelling. A likely reason is the low pH (3.0) of the crystallization buffer in which the groups interacting with the calcium ions are not charged.

About this Structure

2IZW is a Single protein structure of sequence from Ryegrass mottle virus. Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of ryegrass mottle virus at 2.9 A resolution., Plevka P, Tars K, Zeltins A, Balke I, Truve E, Liljas L, Virology. 2007 Dec 20;369(2):364-74. Epub 2007 Sep 19. PMID:17881031 Page seeded by OCA on Sun May 4 08:08:21 2008

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