1x35: Difference between revisions

Revision as of 21:15, 28 July 2008

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File:1x35.png

Template:STRUCTURE 1x35

Recombinant T=3 capsid of a site specific mutant of SeMV CPRecombinant T=3 capsid of a site specific mutant of SeMV CP

Template:ABSTRACT PUBMED 16204893

About this StructureAbout this Structure

1X35 is a Single protein structure of sequence from Sesbania mosaic virus. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies on recombinant T = 3 capsids of Sesbania mosaic virus coat protein mutants., Sangita V, Lokesh GL, Satheshkumar PS, Saravanan V, Vijay CS, Savithri HS, Murthy MR, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1402-5. Epub 2005, Sep 28. PMID:16204893

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Recombinant T=3 capsid of a site specific mutant of SeMV CP'''
+===Recombinant T=3 capsid of a site specific mutant of SeMV CP===
-==Overview==
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-When expressed in Escherichia coli, the recombinant coat protein (rCP) of Sesbania mosaic virus (SeMV) was shown to self-assemble into T = 3 capsids encapsidating CP mRNA and 23S rRNA derived from the host. Expression of CP-P53A, in which a conserved proline at position 53 in the beta-annulus was substituted by alanine (CP-P53A), also produced similar capsids. Purified rCP and CP-P53A particles were crystallized and X-ray crystal structures of their mutant capsids were determined to resolutions of 3.6 and 4.1 A, respectively. As in the native viral CP, the CPs in these recombinant capsids adopt the jelly-roll beta-sandwich fold. The amino-terminal residues of the C subunits alone are ordered and form the beta-annulus structure at the quasi-sixfold axes. A characteristic bend in the beta-annulus remains unaffected in CP-P53A. The quasi-threefold interfaces of the capsids harbour calcium ions coordinated by ligands from the adjacent threefold-related subunits in a geometry that is analogous to that observed in the native capsid. Taken together with studies on deletion and substitution mutants of SeMV CP, these results suggest the possibility that the beta-annulus and nucleic acid-mediated interactions may be less important for the assembly of sobemoviruses than previously envisaged.
+The line below this paragraph, {{ABSTRACT_PUBMED_16204893}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16204893}}
 ==About this Structure==
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 [[Category: Icosahedral virus]]
 [[Category: T=3 capsid]]
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