1slq: Difference between revisions
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[[Image:1slq.gif|left|200px]] | [[Image:1slq.gif|left|200px]] | ||
'''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT''' | {{Structure | ||
|PDB= 1slq |SIZE=350|CAPTION= <scene name='initialview01'>1slq</scene>, resolution 3.2Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= gene segment 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10969 Rhesus rotavirus]) | |||
}} | |||
'''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SLQ is a [ | 1SLQ is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15329727 15329727] | ||
[[Category: Rhesus rotavirus]] | [[Category: Rhesus rotavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: spike protein]] | [[Category: spike protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:06:36 2008'' | ||
Revision as of 12:06, 20 March 2008
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| 1slq, resolution 3.2Å | |||||||||||||
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| Gene: | gene segment 4 (Rhesus rotavirus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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