1slq
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1slq.gif|left|200px]] | [[Image:1slq.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1slq", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1slq| PDB=1slq | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT''' | '''Crystal structure of the trimeric state of the rhesus rotavirus VP4 membrane interaction domain, VP5CT''' | ||
| Line 29: | Line 26: | ||
[[Category: Nason, E B.]] | [[Category: Nason, E B.]] | ||
[[Category: Prasad, B V.V.]] | [[Category: Prasad, B V.V.]] | ||
| - | [[Category: | + | [[Category: Alpha helical triple coiled-coil]] |
| - | [[Category: | + | [[Category: Beta sandwich]] |
| - | [[Category: | + | [[Category: Greek key]] |
| - | [[Category: | + | [[Category: Membrane penetration protein]] |
| - | [[Category: | + | [[Category: Non-enveloped virus]] |
| - | [[Category: | + | [[Category: Spike protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:51:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:51, 3 May 2008
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 Page seeded by OCA on Sat May 3 08:51:37 2008
