5a33

From Proteopedia

(Difference between revisions)

Revision as of 12:37, 23 December 2015

Electron cryo-microscopy of Cowpea Mosaic Virus (CPMV) empty virus like particle (eVLP)

Structural highlights

5a33 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5a32
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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]

Publication Abstract from PubMed

Cowpea mosaic virus is a plant-infecting member of the Picornavirales and is of major interest in the development of biotechnology applications. Despite the availability of >100 crystal structures of Picornavirales capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 A and 3.0 A resolution, respectively, and built de novo atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which was missing from previously determined crystal structures, as well as residues that bind to the viral genome. These observations allow us to develop a new model for genome encapsidation and capsid assembly.

Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM.,Hesketh EL, Meshcheriakova Y, Dent KC, Saxena P, Thompson RF, Cockburn JJ, Lomonossoff GP, Ranson NA Nat Commun. 2015 Dec 10;6:10113. doi: 10.1038/ncomms10113. PMID:26657148^[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:http://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:http://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:http://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:http://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
↑ Hesketh EL, Meshcheriakova Y, Dent KC, Saxena P, Thompson RF, Cockburn JJ, Lomonossoff GP, Ranson NA. Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM. Nat Commun. 2015 Dec 10;6:10113. doi: 10.1038/ncomms10113. PMID:26657148 doi:http://dx.doi.org/10.1038/ncomms10113

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5a33"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Electron cryo-microscopy of Cowpea Mosaic Virus (CPMV) empty virus like particle (eVLP)==
+<StructureSection load='5a33' size='340' side='right' caption='[[5a33]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5a33]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A33 FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a32|5a32]]</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=5a33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a33 OCA], [http://pdbe.org/5a33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a33 RCSB], [http://www.ebi.ac.uk/pdbsum/5a33 PDBsum]</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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cowpea mosaic virus is a plant-infecting member of the Picornavirales and is of major interest in the development of biotechnology applications. Despite the availability of &gt;100 crystal structures of Picornavirales capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 A and 3.0 A resolution, respectively, and built de novo atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which was missing from previously determined crystal structures, as well as residues that bind to the viral genome. These observations allow us to develop a new model for genome encapsidation and capsid assembly.
-The entry 5a33 is ON HOLD  until Paper Publication
+Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM.,Hesketh EL, Meshcheriakova Y, Dent KC, Saxena P, Thompson RF, Cockburn JJ, Lomonossoff GP, Ranson NA Nat Commun. 2015 Dec 10;6:10113. doi: 10.1038/ncomms10113. PMID:26657148<ref>PMID:26657148</ref>
-Authors: Hesketh, E.L., Meshcheriakova, Y., Dent, K.C., Saxena, P., Thompson, R., Cockburn, J.J., Lomonossoff, G.P., Ranson, N.A.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Electron cryo-microscopy of Cowpea Mosaic Virus (CPMV) empty virus like particle (eVLP)
+<div class="pdbe-citations 5a33" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Cockburn, J J]]
+[[Category: Dent, K C]]
+[[Category: Hesketh, E L]]
+[[Category: Lomonossoff, G P]]
+[[Category: Meshcheriakova, Y]]
+[[Category: Ranson, N A]]
 [[Category: Saxena, P]]
-[[Category: Hesketh, E.L]]
-[[Category: Ranson, N.A]]
 [[Category: Thompson, R]]
-[[Category: Cockburn, J.J]]
+[[Category: Comoviridae]]
-[[Category: Dent, K.C]]
+[[Category: Cpmv]]
-[[Category: Lomonossoff, G.P]]
+[[Category: Evlp]]
-[[Category: Meshcheriakova, Y]]
+[[Category: Picornavirales]]
+[[Category: Virus]]

5a33

From Proteopedia

Revision as of 12:37, 23 December 2015

Electron cryo-microscopy of Cowpea Mosaic Virus (CPMV) empty virus like particle (eVLP)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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