1yc6: Difference between revisions
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{{STRUCTURE_1yc6| PDB=1yc6 | SCENE= }} | |||
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'''Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus''' | '''Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus''' | ||
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[[Category: Lucas, R W.]] | [[Category: Lucas, R W.]] | ||
[[Category: McPherson, A.]] | [[Category: McPherson, A.]] | ||
[[Category: | [[Category: Almv]] | ||
[[Category: | [[Category: Assembly]] | ||
[[Category: | [[Category: Bmv]] | ||
[[Category: | [[Category: Icosahedral virus]] | ||
[[Category: | [[Category: Proteolysis]] | ||
[[Category: | [[Category: Structural transition]] | ||
[[Category: | [[Category: Symmetry]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:08:24 2008'' | |||
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Revision as of 13:08, 3 May 2008
Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus
Overview
T=1 icosahedral particles of amino terminally truncated brome mosaic virus (BMV) protein were created by treatment of the wild-type T=3 virus with 1M CaCl2 and crystallized from sodium malonate. Diffraction data were collected from frozen crystals to beyond 2.9 A resolution and the structure determined by molecular replacement and phase extension. The particles are composed of pentameric capsomeres from the wild-type virions which have reoriented with respect to the original particle pentameric axes by rotations of 37 degrees , and formed tenuous interactions with one another, principally through conformationally altered C-terminal polypeptides. Otherwise, the pentamers are virtually superimposable upon those of the original T=3 BMV particles. The T=1 particles, in the crystals, are not perfect icosahedra, but deviate slightly from exact symmetry, possibly due to packing interactions. This suggests that the T=1 particles are deformable, which is consistent with the loose arrangement of pentamers and latticework of holes that penetrate the surface. Atomic force microscopy showed that the T=3 to T=1 transition could occur by shedding of hexameric capsomeres and restructuring of remaining pentamers accompanied by direct condensation. Knowledge of the structures of the BMV wild-type and T=1 particles now permit us to propose a tentative model for that process. A comparison of the BMV T=1 particles was made with the reassembled T=1 particles produced from the coat protein of trypsin treated alfalfa mosaic virus (AlMV), another bromovirus. There is little resemblance between the two particles. The BMV particle, with a maximum diameter of 195 A, is made from distinctive pentameric capsomeres with large holes along the 3-fold axis, while the AlMV particle, of approximate maximum diameter 220 A, has subunits closely packed around the 3-fold axis, large holes along the 5-fold axis, and few contacts within pentamers. In both particles crucial linkages are made about icosahedral dyads.
About this Structure
1YC6 is a Single protein structure of sequence from Brome mosaic virus. Full crystallographic information is available from OCA.
Reference
Crystallographic structure of the T=1 particle of brome mosaic virus., Larson SB, Lucas RW, McPherson A, J Mol Biol. 2005 Feb 25;346(3):815-31. Epub 2005 Jan 12. PMID:15713465 Page seeded by OCA on Sat May 3 16:08:24 2008
