6rrt: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:


==T=4 MS2 Virus-like-particle==
==T=4 MS2 Virus-like-particle==
<StructureSection load='6rrt' size='340' side='right'caption='[[6rrt]]' scene=''>
<StructureSection load='6rrt' size='340' side='right'caption='[[6rrt]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RRT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RRT FirstGlance]. <br>
<table><tr><td colspan='2'>[[6rrt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpms2 Bpms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RRT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RRT FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rrt OCA], [http://pdbe.org/6rrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rrt RCSB], [http://www.ebi.ac.uk/pdbsum/6rrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rrt ProSAT]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rrt OCA], [http://pdbe.org/6rrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rrt RCSB], [http://www.ebi.ac.uk/pdbsum/6rrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rrt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2]] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriophage MS2 is a positive-sense, single-stranded RNA virus encapsulated in an asymmetric T = 3 pseudo-icosahedral capsid. It infects Escherichia coli through the F-pilus, in which it binds through a maturation protein incorporated into its capsid. Cryogenic electron microscopy has previously shown that its genome is highly ordered within virions, and that it regulates the assembly process of the capsid. In this study, we have assembled recombinant MS2 capsids with non-genomic RNA containing the capsid incorporation sequence, and investigated the structures formed, revealing that T = 3, T = 4 and mixed capsids between these two triangulation numbers are generated, and resolving structures of T = 3 and T = 4 capsids to 4 A and 6 A respectively. We conclude that the basic MS2 capsid can form a mix of T = 3 and T = 4 structures, supporting a role for the ordered genome in favouring the formation of functional T = 3 virions.
Bacteriophage MS2 displays unreported capsid variability assembling T = 4 and mixed capsids.,de Martin Garrido N, Crone MA, Ramlaul K, Simpson PA, Freemont PS, Aylett CHS Mol Microbiol. 2020 Jan;113(1):143-152. doi: 10.1111/mmi.14406. Epub 2019 Nov 5. PMID:31618483<ref>PMID:31618483</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rrt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpms2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aylett CHS]]
[[Category: Aylett, C H.S]]
[[Category: Crone MA]]
[[Category: Crone, M A]]
[[Category: Freemont PS]]
[[Category: Freemont, P S]]
[[Category: Ramlaul K]]
[[Category: Garrido, N de Martin]]
[[Category: Simpson PA]]
[[Category: Ramlaul, K]]
[[Category: De Martin Garrido N]]
[[Category: Simpson, P A]]
[[Category: Bacteriophage]]
[[Category: Ms2]]
[[Category: T=4]]
[[Category: Virus like particle]]
[[Category: Vlp]]

Revision as of 14:25, 22 July 2020

T=4 MS2 Virus-like-particleT=4 MS2 Virus-like-particle

Structural highlights

6rrt is a 4 chain structure with sequence from Bpms2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CAPSD_BPMS2] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.[1] [2] [3] [4] [5] [6]

Publication Abstract from PubMed

Bacteriophage MS2 is a positive-sense, single-stranded RNA virus encapsulated in an asymmetric T = 3 pseudo-icosahedral capsid. It infects Escherichia coli through the F-pilus, in which it binds through a maturation protein incorporated into its capsid. Cryogenic electron microscopy has previously shown that its genome is highly ordered within virions, and that it regulates the assembly process of the capsid. In this study, we have assembled recombinant MS2 capsids with non-genomic RNA containing the capsid incorporation sequence, and investigated the structures formed, revealing that T = 3, T = 4 and mixed capsids between these two triangulation numbers are generated, and resolving structures of T = 3 and T = 4 capsids to 4 A and 6 A respectively. We conclude that the basic MS2 capsid can form a mix of T = 3 and T = 4 structures, supporting a role for the ordered genome in favouring the formation of functional T = 3 virions.

Bacteriophage MS2 displays unreported capsid variability assembling T = 4 and mixed capsids.,de Martin Garrido N, Crone MA, Ramlaul K, Simpson PA, Freemont PS, Aylett CHS Mol Microbiol. 2020 Jan;113(1):143-152. doi: 10.1111/mmi.14406. Epub 2019 Nov 5. PMID:31618483[7]

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

References

  1. ↑ Horn WT, Tars K, Grahn E, Helgstrand C, Baron AJ, Lago H, Adams CJ, Peabody DS, Phillips SE, Stonehouse NJ, Liljas L, Stockley PG. Structural basis of RNA binding discrimination between bacteriophages Qbeta and MS2. Structure. 2006 Mar;14(3):487-95. PMID:16531233 doi:http://dx.doi.org/10.1016/j.str.2005.12.006
  2. ↑ Plevka P, Tars K, Liljas L. Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles. Protein Sci. 2008 Oct;17(10):1731-9. Epub 2008 Jul 28. PMID:18662904 doi:10.1110/ps.036905.108
  3. ↑ Rolfsson O, Middleton S, Manfield IW, White SJ, Fan B, Vaughan R, Ranson NA, Dykeman E, Twarock R, Ford J, Kao CC, Stockley PG. Direct Evidence for Packaging Signal-Mediated Assembly of Bacteriophage MS2. J Mol Biol. 2016 Jan 29;428(2 Pt B):431-48. doi: 10.1016/j.jmb.2015.11.014. Epub , 2015 Dec 1. PMID:26608810 doi:http://dx.doi.org/10.1016/j.jmb.2015.11.014
  4. ↑ Golmohammadi R, Valegard K, Fridborg K, Liljas L. The refined structure of bacteriophage MS2 at 2.8 A resolution. J Mol Biol. 1993 Dec 5;234(3):620-39. PMID:8254664 doi:http://dx.doi.org/10.1006/jmbi.1993.1616
  5. ↑ Valegard K, Murray JB, Stonehouse NJ, van den Worm S, Stockley PG, Liljas L. The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions. J Mol Biol. 1997 Aug 1;270(5):724-38. PMID:9245600 doi:http://dx.doi.org/10.1006/jmbi.1997.1144
  6. ↑ van den Worm SH, Stonehouse NJ, Valegard K, Murray JB, Walton C, Fridborg K, Stockley PG, Liljas L. Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments. Nucleic Acids Res. 1998 Mar 1;26(5):1345-51. PMID:9469847
  7. ↑ de Martin Garrido N, Crone MA, Ramlaul K, Simpson PA, Freemont PS, Aylett CHS. Bacteriophage MS2 displays unreported capsid variability assembling T = 4 and mixed capsids. Mol Microbiol. 2020 Jan;113(1):143-152. doi: 10.1111/mmi.14406. Epub 2019 Nov 5. PMID:31618483 doi:http://dx.doi.org/10.1111/mmi.14406

6rrt, resolution 6.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=6rrt&oldid=3269077"