Cowpea Chlorotic Mottle Virus
From Proteopedia
(→Self-Assembling Cowpea Chlorotic Mottle Virus Capsid: Nanoreactor and Scaffold for Molecular Synthesis) |
(→Self-Assembling Cowpea Chlorotic Mottle Virus Capsid: Nanoreactor and Scaffold for Molecular Synthesis) |
||
| Line 2: | Line 2: | ||
===Self-Assembling Cowpea Chlorotic Mottle Virus Capsid: Nanoreactor and Scaffold for Molecular Synthesis=== | ===Self-Assembling Cowpea Chlorotic Mottle Virus Capsid: Nanoreactor and Scaffold for Molecular Synthesis=== | ||
| + | |||
| + | '''Introduction''' | ||
| + | |||
| + | |||
| + | |||
<scene name='Cowpea_Chlorotic_Mottle_Virus/Full_capsid/2'>Assembled Capsid</scene> | <scene name='Cowpea_Chlorotic_Mottle_Virus/Full_capsid/2'>Assembled Capsid</scene> | ||
| Line 13: | Line 18: | ||
<scene name='Cowpea_Chlorotic_Mottle_Virus/Isolated_rna/1'>Isolated RNA</scene> | <scene name='Cowpea_Chlorotic_Mottle_Virus/Isolated_rna/1'>Isolated RNA</scene> | ||
| - | <scene name='Cowpea_Chlorotic_Mottle_Virus/Interior_of_beta_barrel/1'>Interior of Beta Barrel</scene> | + | |
| + | '''General Capsid Structure''' | ||
| + | |||
| + | The viral capsid of CCMV is a complex of proteins stabilized by metal coordination between capsomeres and RNA binding on its internal surface. The viral genome encodes three capsid proteins that are chemically identical. These proteins, arbitrarily called A, B, and C, dimerize with each other and form the capsid's subunits. These subunits then assemble into hexamers and pentamers that comprise the viral capsomeres. The complete capsid structure takes the form of a truncated icosahedron (20 faces). It is described as a T=3 capsid, where the T value is an indicator of structural complexity. | ||
| + | |||
| + | '''Capsomere Structure''' | ||
| + | |||
| + | Hexamers are formed from intercalating B and C subunits which are clasped together by invading carboxy domains. Pentamer capsomeres, on the other hand, are formed exclusively from the contribution of A subunit chains. | ||
| + | |||
| + | Each hexamer is formed from 6 Beta strands that run parallel to each other and result in a pore in the center of the hexamer. Residues 29-33 line this pore and cover the opening of the capsid by the interaction of their side chains with adjacent residues. For example, the "side chain oxygens of Gln29 residues | ||
| + | In the <scene name='Cowpea_Chlorotic_Mottle_Virus/Interior_of_beta_barrel/1'>Interior of Beta Barrel</scene> we see glutamine 29 (in red), valine 31 (in orange), and valine 33 (in green) | ||
| + | |||
| + | |||
| + | |||
| + | |||
| + | |||
| + | |||
| - | STRUCTURES OF THE NATIVE AND SWOLLEN FORMS OF COWPEA CHLOROTIC MOTTLE VIRUS DETERMINED BY X-RAY CRYSTALLOGRAPHY AND CRYO-ELECTRON MICROSCOPY | + | *All Structural Content Derived from Speir et al. |
| + | "STRUCTURES OF THE NATIVE AND SWOLLEN FORMS OF COWPEA CHLOROTIC MOTTLE VIRUS DETERMINED BY X-RAY CRYSTALLOGRAPHY AND CRYO-ELECTRON MICROSCOPY" | ||
Revision as of 04:38, 29 November 2011
|
Self-Assembling Cowpea Chlorotic Mottle Virus Capsid: Nanoreactor and Scaffold for Molecular Synthesis
Introduction
General Capsid Structure
The viral capsid of CCMV is a complex of proteins stabilized by metal coordination between capsomeres and RNA binding on its internal surface. The viral genome encodes three capsid proteins that are chemically identical. These proteins, arbitrarily called A, B, and C, dimerize with each other and form the capsid's subunits. These subunits then assemble into hexamers and pentamers that comprise the viral capsomeres. The complete capsid structure takes the form of a truncated icosahedron (20 faces). It is described as a T=3 capsid, where the T value is an indicator of structural complexity.
Capsomere Structure
Hexamers are formed from intercalating B and C subunits which are clasped together by invading carboxy domains. Pentamer capsomeres, on the other hand, are formed exclusively from the contribution of A subunit chains.
Each hexamer is formed from 6 Beta strands that run parallel to each other and result in a pore in the center of the hexamer. Residues 29-33 line this pore and cover the opening of the capsid by the interaction of their side chains with adjacent residues. For example, the "side chain oxygens of Gln29 residues In the we see glutamine 29 (in red), valine 31 (in orange), and valine 33 (in green)
- All Structural Content Derived from Speir et al.
"STRUCTURES OF THE NATIVE AND SWOLLEN FORMS OF COWPEA CHLOROTIC MOTTLE VIRUS DETERMINED BY X-RAY CRYSTALLOGRAPHY AND CRYO-ELECTRON MICROSCOPY"
Proteopedia Page Contributors and Editors (what is this?)
Inna Blyakhman, Michal Harel, Alexander Berchansky, Joel L. Sussman
