2bfu: Difference between revisions

Revision as of 13:37, 13 October 2021

X-ray structure of CPMV top component

Structural highlights

2bfu is a 2 chain structure with sequence from Cowpea mosaic virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1ny7, 1bmv
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[POL2_CPMVS] Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. Binds to GTP and to single-stranded RNA and single-stranded DNA in a non-sequence-specific manner.^[1] ^[2] ^[3] ^[4] The cleavable C-terminus of small coat protein seems to be involved in the packaging of the virion RNAs. Also seems to act as suppressor of post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs.^[5] ^[6] ^[7] ^[8]

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

Chemical and genetic modifications on the surface of viral protein cages confer unique properties to the virus particles with potential nano and biotechnological applications. The enclosed space in the interior of the virus particles further increases its versatility as a nanomaterial. In this paper, we report a simple method to generate a high yield of stable cowpea mosaic virus (CPMV) empty capsids from their native nucleoprotein counterparts by removing the encapsidated viral genome without compromising the integrity of the protein coat. Biochemical and structural comparison of artificially generated empty particles did not reveal any distinguishable differences from CPMV particles containing viral RNA. Preliminary results on the use of artificially produced empty CPMV capsids as a carrier capsule are described.

Generation and structural analysis of reactive empty particles derived from an icosahedral virus.,Ochoa WF, Chatterji A, Lin T, Johnson JE Chem Biol. 2006 Jul;13(7):771-8. PMID:16873025^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Taylor KM, Spall VE, Butler PJ, Lomonossoff GP. The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. Virology. 1999 Mar 1;255(1):129-37. PMID:10049828
↑ Canizares MC, Taylor KM, Lomonossoff GP. Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing. J Gen Virol. 2004 Nov;85(Pt 11):3431-5. PMID:15483261 doi:https://dx.doi.org/85/11/3431
↑ Liu L, Grainger J, Canizares MC, Angell SM, Lomonossoff GP. Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be counteracted by a RNA-2-encoded suppressor of silencing. Virology. 2004 May 20;323(1):37-48. PMID:15165817 doi:https://dx.doi.org/10.1016/j.virol.2004.02.013
↑ Carvalho CM, Pouwels J, van Lent JW, Bisseling T, Goldbach RW, Wellink J. The movement protein of cowpea mosaic virus binds GTP and single-stranded nucleic acid in vitro. J Virol. 2004 Feb;78(3):1591-4. PMID:14722313
↑ Taylor KM, Spall VE, Butler PJ, Lomonossoff GP. The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. Virology. 1999 Mar 1;255(1):129-37. PMID:10049828
↑ Canizares MC, Taylor KM, Lomonossoff GP. Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing. J Gen Virol. 2004 Nov;85(Pt 11):3431-5. PMID:15483261 doi:https://dx.doi.org/85/11/3431
↑ Liu L, Grainger J, Canizares MC, Angell SM, Lomonossoff GP. Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be counteracted by a RNA-2-encoded suppressor of silencing. Virology. 2004 May 20;323(1):37-48. PMID:15165817 doi:https://dx.doi.org/10.1016/j.virol.2004.02.013
↑ Carvalho CM, Pouwels J, van Lent JW, Bisseling T, Goldbach RW, Wellink J. The movement protein of cowpea mosaic virus binds GTP and single-stranded nucleic acid in vitro. J Virol. 2004 Feb;78(3):1591-4. PMID:14722313
↑ Ochoa WF, Chatterji A, Lin T, Johnson JE. Generation and structural analysis of reactive empty particles derived from an icosahedral virus. Chem Biol. 2006 Jul;13(7):771-8. PMID:16873025 doi:10.1016/j.chembiol.2006.05.014

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OCA

[1] Taylor KM, Spall VE, Butler PJ, Lomonossoff GP. The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. Virology. 1999 Mar 1;255(1):129-37. PMID:10049828

[2] Canizares MC, Taylor KM, Lomonossoff GP. Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing. J Gen Virol. 2004 Nov;85(Pt 11):3431-5. PMID:15483261 doi:https://dx.doi.org/85/11/3431

[3] Liu L, Grainger J, Canizares MC, Angell SM, Lomonossoff GP. Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be counteracted by a RNA-2-encoded suppressor of silencing. Virology. 2004 May 20;323(1):37-48. PMID:15165817 doi:https://dx.doi.org/10.1016/j.virol.2004.02.013

[4] Carvalho CM, Pouwels J, van Lent JW, Bisseling T, Goldbach RW, Wellink J. The movement protein of cowpea mosaic virus binds GTP and single-stranded nucleic acid in vitro. J Virol. 2004 Feb;78(3):1591-4. PMID:14722313

[5] Taylor KM, Spall VE, Butler PJ, Lomonossoff GP. The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. Virology. 1999 Mar 1;255(1):129-37. PMID:10049828

[6] Canizares MC, Taylor KM, Lomonossoff GP. Surface-exposed C-terminal amino acids of the small coat protein of Cowpea mosaic virus are required for suppression of silencing. J Gen Virol. 2004 Nov;85(Pt 11):3431-5. PMID:15483261 doi:https://dx.doi.org/85/11/3431

[7] Liu L, Grainger J, Canizares MC, Angell SM, Lomonossoff GP. Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be counteracted by a RNA-2-encoded suppressor of silencing. Virology. 2004 May 20;323(1):37-48. PMID:15165817 doi:https://dx.doi.org/10.1016/j.virol.2004.02.013

[8] Carvalho CM, Pouwels J, van Lent JW, Bisseling T, Goldbach RW, Wellink J. The movement protein of cowpea mosaic virus binds GTP and single-stranded nucleic acid in vitro. J Virol. 2004 Feb;78(3):1591-4. PMID:14722313

[9] Ochoa WF, Chatterji A, Lin T, Johnson JE. Generation and structural analysis of reactive empty particles derived from an icosahedral virus. Chem Biol. 2006 Jul;13(7):771-8. PMID:16873025 doi:10.1016/j.chembiol.2006.05.014

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@@ Line 3: / Line 3: @@
 <StructureSection load='2bfu' size='340' side='right'caption='[[2bfu]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bfu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cowpea_mosaic_virus Cowpea mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bfu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cowpea_mosaic_virus Cowpea mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFU FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ny7|1ny7]], [[1bmv|1bmv]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ny7|1ny7]], [[1bmv|1bmv]]</div></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=2bfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfu OCA], [http://pdbe.org/2bfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bfu RCSB], [http://www.ebi.ac.uk/pdbsum/2bfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfu ProSAT]</span></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=2bfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfu OCA], [https://pdbe.org/2bfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfu RCSB], [https://www.ebi.ac.uk/pdbsum/2bfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/POL2_CPMVS POL2_CPMVS]] Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. Binds to GTP and to single-stranded RNA and single-stranded DNA in a non-sequence-specific manner.<ref>PMID:10049828</ref> <ref>PMID:15483261</ref> <ref>PMID:15165817</ref> <ref>PMID:14722313</ref>   The cleavable C-terminus of small coat protein seems to be involved in the packaging of the virion RNAs. Also seems to act as suppressor of post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs.<ref>PMID:10049828</ref> <ref>PMID:15483261</ref> <ref>PMID:15165817</ref> <ref>PMID:14722313</ref>
+[[https://www.uniprot.org/uniprot/POL2_CPMVS POL2_CPMVS]] Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids. Binds to GTP and to single-stranded RNA and single-stranded DNA in a non-sequence-specific manner.<ref>PMID:10049828</ref> <ref>PMID:15483261</ref> <ref>PMID:15165817</ref> <ref>PMID:14722313</ref>   The cleavable C-terminus of small coat protein seems to be involved in the packaging of the virion RNAs. Also seems to act as suppressor of post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs.<ref>PMID:10049828</ref> <ref>PMID:15483261</ref> <ref>PMID:15165817</ref> <ref>PMID:14722313</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
 *[[Cowpea Chlorotic Mottle Virus|Cowpea Chlorotic Mottle Virus]]
-*[[Virus coat protein|Virus coat protein]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>

2bfu: Difference between revisions

Revision as of 13:37, 13 October 2021

X-ray structure of CPMV top component

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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