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4bp7

From Proteopedia

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Current revision

Asymmetric structure of a virus-receptor complex

4bp7, resolution 39.00Å

Structural highlights

4bp7 is a 180 chain structure with sequence from Escherichia virus MS2. This structure supersedes the now removed PDB entries 4bp4, 4bp5 and 4bp6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 39Å
Experimental data:	Check to display Experimental Data
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

Simple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and their genomes, which are vital for infection. Here, we report an asymmetric structure of bacteriophage MS2, attached to its receptor, the F-pilus. Cryo-electron tomography and subtomographic averaging of such complexes result in a structure containing clear density for the packaged genome, implying that the conformation of the genome is the same in each virus particle. The data also suggest that the single-copy viral maturation protein breaks the symmetry of the capsid, occupying a position that would be filled by a coat protein dimer in an icosahedral shell. This capsomere can thus fulfill its known biological roles in receptor and genome binding and suggests an exit route for the genome during infection.

The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release.,Dent KC, Thompson R, Barker AM, Hiscox JA, Barr JN, Stockley PG, Ranson NA Structure. 2013 Jun 25. pii: S0969-2126(13)00194-9. doi:, 10.1016/j.str.2013.05.012. PMID:23810697^[7]

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

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Dent KC, Thompson R, Barker AM, Hiscox JA, Barr JN, Stockley PG, Ranson NA. The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release. Structure. 2013 Jun 25. pii: S0969-2126(13)00194-9. doi:, 10.1016/j.str.2013.05.012. PMID:23810697 doi:10.1016/j.str.2013.05.012

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bp7"

@@ Line 1: / Line 1: @@
-<div  style="background-color:yellow;" border="1" cellpadding="5">''Warning: this is a large structure, and loading might take a long time or not happen at all.''</div>
+==Asymmetric structure of a virus-receptor complex==
-== Asymmetric structure of a virus-receptor complex ==
+<SX load='4bp7' size='340' side='right' viewer='molstar' caption='[[4bp7]], [[Resolution|resolution]] 39.00&Aring;' scene=''>
-[[Image:4bp7.jpg]]
+== Structural highlights ==
-[[4bp7]] is a 176 chain structure, available for rendering on Proteopedia in 3 parts.
+<table><tr><td colspan='2'>[[4bp7]] is a 180 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_MS2 Escherichia virus MS2]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bp4 4bp4], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bp5 4bp5] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bp6 4bp6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BP7 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 39&#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=4bp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bp7 OCA], [https://pdbe.org/4bp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bp7 RCSB], [https://www.ebi.ac.uk/pdbsum/4bp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bp7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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 ==
@@ Line 12: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4bp7" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>
-[[Category: Hiscox, J.A]]
+__TOC__
-[[Category: Dent, K.C]]
+</SX>
-[[Category: Barker, A.M]]
+[[Category: Escherichia virus MS2]]
-[[Category: Ranson, N.A]]
+[[Category: Large Structures]]
-[[Category: Barr, J.N]]
+[[Category: Barker AM]]
-[[Category: Stockley, P.G]]
+[[Category: Barr JN]]
-[[Category: Thompson, R]]
+[[Category: Dent KC]]
+[[Category: Hiscox JA]]
+[[Category: Ranson NA]]
+[[Category: Stockley PG]]
+[[Category: Thompson R]]

4bp7

From Proteopedia

Current revision

Asymmetric structure of a virus-receptor complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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