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Cowpea Chlorotic Mottle Virus

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(→Self-Assembling Cowpea Chlorotic Mottle Virus Capsid: Nanoreactor and Scaffold for Molecular Synthesis)
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<Structure load='1CWP' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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<StructureSection load='' size='350' side='right' caption='Cowpea chlorotic mottle virus coast protein trimer complex with RNA (PDB entry [[1cwp]])' scene='47/472643/Cv/1'>
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== Function ==
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===Self-Assembling Cowpea Chlorotic Mottle Virus Capsid: Nanoreactor and Scaffold for Molecular Synthesis===
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'''Cowpea chlorotic mottle virus''' (CPMV) infects black-eyed pea plants. The CPMV is composed of protein shell (capsid) and RNA.
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<scene name='47/472643/Cv/2'>Cowpea chlorotic mottle virus coast protein trimer with RNA</scene> (PDB entry [[1cwp]]).
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== Relevance ==
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'''Introduction'''
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CPMV is used in nanotechnology due to its pH and metal ion-dependent polymorphism which can be used for delivery of small molecules. <ref>PMID:7743132</ref>
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</StructureSection>
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==3D structures of CPMV==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[1ny7]], [[2bfu]] – CPMV small + large subunits<br />
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[[1cwp]] – CPMV coat protein + RNA<br />
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[[1za7]] – CPMV coat protein (mutant)<br />
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== References ==
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<references/>
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<scene name='Cowpea_Chlorotic_Mottle_Virus/Full_capsid/2'>Assembled Capsid</scene>
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[[Category:Topic Page]]
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<scene name='Cowpea_Chlorotic_Mottle_Virus/Protein_and_rna/1'>Protein Core with Stabilizing RNA Interactions</scene>
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<scene name='Cowpea_Chlorotic_Mottle_Virus/Isolated_rna/1'>Isolated RNA</scene>
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'''General Capsid Structure'''
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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.
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'''Capsomere Structure'''
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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.
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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
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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)
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*All Structural Content Derived from Speir et al.
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"STRUCTURES OF THE NATIVE AND SWOLLEN FORMS OF COWPEA CHLOROTIC MOTTLE VIRUS DETERMINED BY X-RAY CRYSTALLOGRAPHY AND CRYO-ELECTRON MICROSCOPY"
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Current revision

Cowpea chlorotic mottle virus coast protein trimer complex with RNA (PDB entry 1cwp)

Drag the structure with the mouse to rotate

3D structures of CPMV

Updated on 16-May-2019

1ny7, 2bfu – CPMV small + large subunits
1cwp – CPMV coat protein + RNA
1za7 – CPMV coat protein (mutant)

References

  1. ↑ Speir JA, Munshi S, Wang G, Baker TS, Johnson JE. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure. 1995 Jan 15;3(1):63-78. PMID:7743132

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Inna Blyakhman, Michal Harel, Alexander Berchansky, Joel L. Sussman

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