1sva: Difference between revisions
New page: left|200px<br /> <applet load="1sva" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sva, resolution 3.1Å" /> '''SIMIAN VIRUS 40'''<b... |
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[[Image:1sva.gif|left|200px]]<br /> | [[Image:1sva.gif|left|200px]]<br /><applet load="1sva" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1sva, resolution 3.1Å" /> | caption="1sva, resolution 3.1Å" /> | ||
'''SIMIAN VIRUS 40'''<br /> | '''SIMIAN VIRUS 40'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: The structure of simian virus 40 (SV40), previously determined | BACKGROUND: The structure of simian virus 40 (SV40), previously determined at 3.8 degree resolution, shows how its pentameric VP1 assembly units are tied together by extended C-terminal arms. In order to define more precisely the possible assembly mechanisms, we have refined the structure at 3.1 degree resolution. RESULTS: New data from a high-intensity synchrotron source have been used for phase extension by electron-density averaging and refinement, exploiting only the strict 5-fold non-crystallographic symmetry for the real-space averaging steps. The accurate model enables us to study important structural features of the virus particle in detail. The remarkably invariant core of the VP1 pentamer bears the docking sites for the C-terminal arms from other pentamers. These contacts are the principal way in which pentameric assembly units are linked together in the capsid. Only at the interface between five-coordinated and six-coordinated pentamers do the pentamer cores appear to interact strongly. There are two cation-binding sites per VP1 monomer, seen in a soaking experiment with gadolinium nitrate. These sites are quite close to each other at the interfaces between pentamers. CONCLUSION: We propose that the contact between five-coordinated and six-coordinated pentamers may help to generate a six-pentamer nucleus, with which further pentamers can assemble to generate the complete particle. Calcium ions probably stabilize the structure of the assembled particle, rather than direct its assembly. | ||
==About this Structure== | ==About this Structure== | ||
1SVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40]. The following page contains interesting information on the relation of 1SVA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb47_1.html Simian Virus 40]]. Full crystallographic information is available from [http:// | 1SVA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_virus_40 Simian virus 40]. The following page contains interesting information on the relation of 1SVA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb47_1.html Simian Virus 40]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Simian virus 40]] | [[Category: Simian virus 40]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gamblin, S | [[Category: Gamblin, S J.]] | ||
[[Category: Harrison, S | [[Category: Harrison, S C.]] | ||
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
[[Category: virus coat protein]] | [[Category: virus coat protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:35 2008'' | ||
Revision as of 16:05, 21 February 2008
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SIMIAN VIRUS 40
OverviewOverview
BACKGROUND: The structure of simian virus 40 (SV40), previously determined at 3.8 degree resolution, shows how its pentameric VP1 assembly units are tied together by extended C-terminal arms. In order to define more precisely the possible assembly mechanisms, we have refined the structure at 3.1 degree resolution. RESULTS: New data from a high-intensity synchrotron source have been used for phase extension by electron-density averaging and refinement, exploiting only the strict 5-fold non-crystallographic symmetry for the real-space averaging steps. The accurate model enables us to study important structural features of the virus particle in detail. The remarkably invariant core of the VP1 pentamer bears the docking sites for the C-terminal arms from other pentamers. These contacts are the principal way in which pentameric assembly units are linked together in the capsid. Only at the interface between five-coordinated and six-coordinated pentamers do the pentamer cores appear to interact strongly. There are two cation-binding sites per VP1 monomer, seen in a soaking experiment with gadolinium nitrate. These sites are quite close to each other at the interfaces between pentamers. CONCLUSION: We propose that the contact between five-coordinated and six-coordinated pentamers may help to generate a six-pentamer nucleus, with which further pentamers can assemble to generate the complete particle. Calcium ions probably stabilize the structure of the assembled particle, rather than direct its assembly.
About this StructureAbout this Structure
1SVA is a Single protein structure of sequence from Simian virus 40. The following page contains interesting information on the relation of 1SVA with [Simian Virus 40]. Full crystallographic information is available from OCA.
ReferenceReference
The structure of simian virus 40 refined at 3.1 A resolution., Stehle T, Gamblin SJ, Yan Y, Harrison SC, Structure. 1996 Feb 15;4(2):165-82. PMID:8805523
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