1ny7: Difference between revisions

Revision as of 08:54, 10 April 2024

COWPEA MOSAIC VIRUS (CPMV)

Structural highlights

1ny7 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.
Method:	X-ray diffraction, Resolution 3Å
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.

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

Proteopedia Page Contributors and Editors (what is this?)

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

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

@@ Line 3: / Line 3: @@
 <StructureSection load='1ny7' size='340' side='right'caption='[[1ny7]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ny7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cpmv Cpmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NY7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ny7]] 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=1NY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NY7 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bmv|1bmv]]</div></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]] 3&#8491;</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=1ny7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ny7 OCA], [https://pdbe.org/1ny7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ny7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ny7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ny7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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 19: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ny7 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Comoviruses are a group of plant viruses in the picornavirus superfamily. The type member of comoviruses, cowpea mosaic virus (CPMV), was crystallized in the cubic space group I23, a = 317 A and the hexagonal space group P6(1)22, a = 451 A, c = 1038 A. Structures of three closely similar nucleoprotein particles were determined in the cubic form. The roughly 300-A capsid was similar to the picornavirus capsid displaying a pseudo T = 3 (P = 3) surface lattice. The three beta-sandwich domains adopt two orientations, one with the long axis radial and the other two with the long axes tangential in reference to the capsid sphere. T = 3 viruses display one or the other of these two orientations. The CPMV capsid was permeable to cesium ions, leading to a disturbance of the beta-annulus inside a channel-like structure, suggesting an ion channel. The hexagonal crystal form diffracted X rays to 3 A resolution, despite the large unit cell. The large ( approximately 200 A) solvent channels in the lattice allow exchange of CPMV cognate Fab fragments. As an initial step in the structure determination of the CPMV/Fab complex, the P6(1)22 crystal structure was solved by molecular replacement with the CPMV model determined in the cubic cell.
-The refined crystal structure of cowpea mosaic virus at 2.8 A resolution.,Lin T, Chen Z, Usha R, Stauffacher CV, Dai JB, Schmidt T, Johnson JE Virology. 1999 Dec 5;265(1):20-34. PMID:10603314<ref>PMID:10603314</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ny7" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Cpmv]]
+[[Category: Cowpea mosaic virus]]
 [[Category: Large Structures]]
-[[Category: Chen, Z]]
+[[Category: Chen Z]]
-[[Category: Dai, J B]]
+[[Category: Dai J-B]]
-[[Category: Johnson, J E]]
+[[Category: Johnson JE]]
-[[Category: Lin, T]]
+[[Category: Lin T]]
-[[Category: Schmidt, T]]
+[[Category: Schmidt T]]
-[[Category: Stauffacher, C V]]
+[[Category: Stauffacher CV]]
-[[Category: Usha, R]]
+[[Category: Usha R]]
-[[Category: Comovirus]]
-[[Category: Icosahedral virus]]
-[[Category: Viral coat protein]]
-[[Category: Virus]]

1ny7: Difference between revisions

Revision as of 08:54, 10 April 2024

COWPEA MOSAIC VIRUS (CPMV)

Structural highlights

Function

Evolutionary Conservation

See Also

References

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