1slq
From Proteopedia
(New page: 200px<br /><applet load="1slq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1slq, resolution 3.2Å" /> '''Crystal structure of ...) |
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| - | [[Image:1slq.gif|left|200px]]<br /><applet load="1slq" size=" | + | [[Image:1slq.gif|left|200px]]<br /><applet load="1slq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1slq, resolution 3.2Å" /> | caption="1slq, resolution 3.2Å" /> | ||
'''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT'''<br /> | '''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Non-enveloped virus particles (those that lack a lipid-bilayer membrane) | + | Non-enveloped virus particles (those that lack a lipid-bilayer membrane) must breach the membrane of a target host cell to gain access to its cytoplasm. So far, the molecular mechanism of this membrane penetration step has resisted structural analysis. The spike protein VP4 is a principal component in the entry apparatus of rotavirus, a non-enveloped virus that causes gastroenteritis and kills 440,000 children each year. Trypsin cleavage of VP4 primes the virus for entry by triggering a rearrangement that rigidifies the VP4 spikes. We have determined the crystal structure, at 3.2 A resolution, of the main part of VP4 that projects from the virion. The crystal structure reveals a coiled-coil stabilized trimer. Comparison of this structure with the two-fold clustered VP4 spikes in a approximately 12 A resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows that VP4 also undergoes a second rearrangement, in which the oligomer reorganizes and each subunit folds back on itself, translocating a potential membrane-interaction peptide from one end of the spike to the other. This rearrangement resembles the conformational transitions of membrane fusion proteins of enveloped viruses. |
==About this Structure== | ==About this Structure== | ||
| - | 1SLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus]. Full crystallographic information is available from [http:// | + | 1SLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhesus_rotavirus Rhesus rotavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rhesus rotavirus]] | [[Category: Rhesus rotavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dormitzer, P | + | [[Category: Dormitzer, P R.]] |
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
| - | [[Category: Nason, E | + | [[Category: Nason, E B.]] |
| - | [[Category: Prasad, B | + | [[Category: Prasad, B V.V.]] |
[[Category: alpha helical triple coiled-coil]] | [[Category: alpha helical triple coiled-coil]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
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[[Category: spike protein]] | [[Category: spike protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:47 2008'' |
Revision as of 13:02, 21 February 2008
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Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT
Overview
Non-enveloped virus particles (those that lack a lipid-bilayer membrane) must breach the membrane of a target host cell to gain access to its cytoplasm. So far, the molecular mechanism of this membrane penetration step has resisted structural analysis. The spike protein VP4 is a principal component in the entry apparatus of rotavirus, a non-enveloped virus that causes gastroenteritis and kills 440,000 children each year. Trypsin cleavage of VP4 primes the virus for entry by triggering a rearrangement that rigidifies the VP4 spikes. We have determined the crystal structure, at 3.2 A resolution, of the main part of VP4 that projects from the virion. The crystal structure reveals a coiled-coil stabilized trimer. Comparison of this structure with the two-fold clustered VP4 spikes in a approximately 12 A resolution image reconstruction from electron cryomicroscopy of trypsin-primed virions shows that VP4 also undergoes a second rearrangement, in which the oligomer reorganizes and each subunit folds back on itself, translocating a potential membrane-interaction peptide from one end of the spike to the other. This rearrangement resembles the conformational transitions of membrane fusion proteins of enveloped viruses.
About this Structure
1SLQ is a Single protein structure of sequence from Rhesus rotavirus. Full crystallographic information is available from OCA.
Reference
Structural rearrangements in the membrane penetration protein of a non-enveloped virus., Dormitzer PR, Nason EB, Prasad BV, Harrison SC, Nature. 2004 Aug 26;430(7003):1053-8. PMID:15329727
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