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| | ==CRICKET PARALYSIS VIRUS (CRPV)== | | ==CRICKET PARALYSIS VIRUS (CRPV)== |
| - | <StructureSection load='1b35' size='340' side='right' caption='[[1b35]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1b35' size='340' side='right'caption='[[1b35]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b35]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cricket_paralysis_virus Cricket paralysis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B35 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b35]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricket_paralysis_virus Cricket paralysis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B35 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b35 OCA], [http://pdbe.org/1b35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b35 RCSB], [http://www.ebi.ac.uk/pdbsum/1b35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b35 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b35 OCA], [https://pdbe.org/1b35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b35 RCSB], [https://www.ebi.ac.uk/pdbsum/1b35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b35 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/POLS_CRPVC POLS_CRPVC]] Structural polyprotein: precursor of all the viral capsid proteins. Capsid protein 1, together with capsid proteins 2 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 4 is a tstructural component of the icosahedral capsid protecting the genomic RNA. It may play an important role in capsid assembly. Capsid protein 2, together with capsid proteins 1 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 3, together with capsid proteins 1 and 2, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. | + | [https://www.uniprot.org/uniprot/POLS_CRPVC POLS_CRPVC] Structural polyprotein: precursor of all the viral capsid proteins. Capsid protein 1, together with capsid proteins 2 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 4 is a tstructural component of the icosahedral capsid protecting the genomic RNA. It may play an important role in capsid assembly. Capsid protein 2, together with capsid proteins 1 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 3, together with capsid proteins 1 and 2, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/1b35_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/1b35_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Cricket paralysis virus]] | | [[Category: Cricket paralysis virus]] |
| - | [[Category: Christian, P D]] | + | [[Category: Large Structures]] |
| - | [[Category: Johnson, J E]] | + | [[Category: Christian PD]] |
| - | [[Category: Liljas, L]] | + | [[Category: Johnson JE]] |
| - | [[Category: Lin, T W]] | + | [[Category: Liljas L]] |
| - | [[Category: Scotti, P D]] | + | [[Category: Lin TW]] |
| - | [[Category: Tate, J G]] | + | [[Category: Scotti PD]] |
| - | [[Category: Icosahedral virus]]
| + | [[Category: Tate JG]] |
| - | [[Category: Insect picorna-like virus]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
POLS_CRPVC Structural polyprotein: precursor of all the viral capsid proteins. Capsid protein 1, together with capsid proteins 2 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 4 is a tstructural component of the icosahedral capsid protecting the genomic RNA. It may play an important role in capsid assembly. Capsid protein 2, together with capsid proteins 1 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 3, together with capsid proteins 1 and 2, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Numerous small, RNA-containing insect viruses are currently classified as picornaviruses, or as 'picorna-like', since they superficially resemble the true picornaviruses. Considerable evidence now suggests that several of these viruses are members of a distinct family. We have determined the gene sequence of the capsid proteins and the 2.4 A resolution crystal structure of the cricket paralysis virus. While the genome sequence indicates that the insect picorna-like viruses represent a distinct lineage compared to true picornaviruses, the capsid structure demonstrates that the two groups are related. These viral genomes are, thus, best viewed as composed of exchangeable modules that have recombined.
The crystal structure of cricket paralysis virus: the first view of a new virus family.,Tate J, Liljas L, Scotti P, Christian P, Lin T, Johnson JE Nat Struct Biol. 1999 Aug;6(8):765-74. PMID:10426956[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tate J, Liljas L, Scotti P, Christian P, Lin T, Johnson JE. The crystal structure of cricket paralysis virus: the first view of a new virus family. Nat Struct Biol. 1999 Aug;6(8):765-74. PMID:10426956 doi:http://dx.doi.org/10.1038/11543
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