1yc6

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(New page: 200px<br /><applet load="1yc6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yc6, resolution 2.90&Aring;" /> '''Crystallographic Str...)
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caption="1yc6, resolution 2.90&Aring;" />
caption="1yc6, resolution 2.90&Aring;" />
'''Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus'''<br />
'''Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1YC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brome_mosaic_virus Brome mosaic virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YC6 OCA].
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1YC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brome_mosaic_virus Brome mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YC6 OCA].
==Reference==
==Reference==
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[[Category: Brome mosaic virus]]
[[Category: Brome mosaic virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Larson, S.B.]]
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[[Category: Larson, S B.]]
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[[Category: Lucas, R.W.]]
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[[Category: Lucas, R W.]]
[[Category: McPherson, A.]]
[[Category: McPherson, A.]]
[[Category: almv]]
[[Category: almv]]
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[[Category: symmetry]]
[[Category: symmetry]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:40:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:52 2008''

Revision as of 14:03, 21 February 2008


1yc6, resolution 2.90Å

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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

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