1pov: Difference between revisions
New page: left|200px<br /><applet load="1pov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pov, resolution 2.8Å" /> '''ROLE AND MECHANISM OF... |
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[[Image:1pov.gif|left|200px]]<br /><applet load="1pov" size=" | [[Image:1pov.gif|left|200px]]<br /><applet load="1pov" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pov, resolution 2.8Å" /> | caption="1pov, resolution 2.8Å" /> | ||
'''ROLE AND MECHANISM OF THE MATURATION CLEAVAGE OF VP0 IN POLIOVIRUS ASSEMBLY: STRUCTURE OF THE EMPTY CAPSID ASSEMBLY INTERMEDIATE AT 2.9 ANGSTROMS RESOLUTION'''<br /> | '''ROLE AND MECHANISM OF THE MATURATION CLEAVAGE OF VP0 IN POLIOVIRUS ASSEMBLY: STRUCTURE OF THE EMPTY CAPSID ASSEMBLY INTERMEDIATE AT 2.9 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the P1/Mahoney poliovirus empty capsid has been | The crystal structure of the P1/Mahoney poliovirus empty capsid has been determined at 2.9 A resolution. The empty capsids differ from mature virions in that they lack the viral RNA and have yet to undergo a stabilizing maturation cleavage of VP0 to yield the mature capsid proteins VP4 and VP2. The outer surface and the bulk of the protein shell are very similar to those of the mature virion. The major differences between the 2 structures are focused in a network formed by the N-terminal extensions of the capsid proteins on the inner surface of the shell. In the empty capsids, the entire N-terminal extension of VP1, as well as portions corresponding to VP4 and the N-terminal extension of VP2, are disordered, and many stabilizing interactions that are present in the mature virion are missing. In the empty capsid, the VP0 scissile bond is located some 20 A away from the positions in the mature virion of the termini generated by VP0 cleavage. The scissile bond is located on the rim of a trefoil-shaped depression in the inner surface of the shell that is highly reminiscent of an RNA binding site in bean pod mottle virus. The structure suggests plausible (and ultimately testable) models for the initiation of encapsidation, for the RNA-dependent autocatalytic cleavage of VP0, and for the role of the cleavage in establishing the ordered N-terminal network and in generating stable virions. | ||
==About this Structure== | ==About this Structure== | ||
1POV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1] with MYR and SPH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1POV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1] with <scene name='pdbligand=MYR:'>MYR</scene> and <scene name='pdbligand=SPH:'>SPH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1POV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Basavappa, R.]] | [[Category: Basavappa, R.]] | ||
[[Category: Filman, D | [[Category: Filman, D J.]] | ||
[[Category: Hogle, J | [[Category: Hogle, J M.]] | ||
[[Category: MYR]] | [[Category: MYR]] | ||
[[Category: SPH]] | [[Category: SPH]] | ||
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[[Category: picornavirus]] | [[Category: picornavirus]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:57 2008'' | ||
Revision as of 15:31, 21 February 2008
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ROLE AND MECHANISM OF THE MATURATION CLEAVAGE OF VP0 IN POLIOVIRUS ASSEMBLY: STRUCTURE OF THE EMPTY CAPSID ASSEMBLY INTERMEDIATE AT 2.9 ANGSTROMS RESOLUTION
OverviewOverview
The crystal structure of the P1/Mahoney poliovirus empty capsid has been determined at 2.9 A resolution. The empty capsids differ from mature virions in that they lack the viral RNA and have yet to undergo a stabilizing maturation cleavage of VP0 to yield the mature capsid proteins VP4 and VP2. The outer surface and the bulk of the protein shell are very similar to those of the mature virion. The major differences between the 2 structures are focused in a network formed by the N-terminal extensions of the capsid proteins on the inner surface of the shell. In the empty capsids, the entire N-terminal extension of VP1, as well as portions corresponding to VP4 and the N-terminal extension of VP2, are disordered, and many stabilizing interactions that are present in the mature virion are missing. In the empty capsid, the VP0 scissile bond is located some 20 A away from the positions in the mature virion of the termini generated by VP0 cleavage. The scissile bond is located on the rim of a trefoil-shaped depression in the inner surface of the shell that is highly reminiscent of an RNA binding site in bean pod mottle virus. The structure suggests plausible (and ultimately testable) models for the initiation of encapsidation, for the RNA-dependent autocatalytic cleavage of VP0, and for the role of the cleavage in establishing the ordered N-terminal network and in generating stable virions.
About this StructureAbout this Structure
1POV is a Protein complex structure of sequences from Human poliovirus 1 with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolution., Basavappa R, Syed R, Flore O, Icenogle JP, Filman DJ, Hogle JM, Protein Sci. 1994 Oct;3(10):1651-69. PMID:7849583
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