|
|
| (4 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Icosahedral particle of covalent coat protein dimer of bacteriophage MS2== | | ==Icosahedral particle of covalent coat protein dimer of bacteriophage MS2== |
| - | <StructureSection load='2wbh' size='340' side='right' caption='[[2wbh]], [[Resolution|resolution]] 4.70Å' scene=''> | + | <StructureSection load='2wbh' size='340' side='right'caption='[[2wbh]], [[Resolution|resolution]] 4.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wbh]] is a 3 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=2WBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WBH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wbh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_MS2 Escherichia virus MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WBH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b2e|2b2e]], [[6msf|6msf]], [[2bs0|2bs0]], [[2iz9|2iz9]], [[7msf|7msf]], [[2b2g|2b2g]], [[2c4q|2c4q]], [[2c4y|2c4y]], [[1zdj|1zdj]], [[2c4z|2c4z]], [[2c51|2c51]], [[2bny|2bny]], [[1u1y|1u1y]], [[2vtu|2vtu]], [[2bs1|2bs1]], [[1msc|1msc]], [[1mvb|1mvb]], [[2izn|2izn]], [[1mst|1mst]], [[1aq4|1aq4]], [[2ms2|2ms2]], [[2c50|2c50]], [[1zdi|1zdi]], [[1zdk|1zdk]], [[1aq3|1aq3]], [[1mva|1mva]], [[5msf|5msf]], [[2b2d|2b2d]], [[1bms|1bms]], [[1zdh|1zdh]], [[1zse|1zse]], [[2bq5|2bq5]], [[2iz8|2iz8]], [[2izm|2izm]], [[2bu1|2bu1]]</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]] 4.7Å</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=2wbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wbh RCSB], [http://www.ebi.ac.uk/pdbsum/2wbh PDBsum]</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=2wbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbh OCA], [https://pdbe.org/2wbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wbh RCSB], [https://www.ebi.ac.uk/pdbsum/2wbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wbh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COAT_BPMS2 COAT_BPMS2]] Forms the phage shell; binds to the phage RNA. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 16: |
Line 17: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2wbh" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpms2]] | + | [[Category: Escherichia virus MS2]] |
| - | [[Category: Liljas, L]] | + | [[Category: Large Structures]] |
| - | [[Category: Plevka, P]] | + | [[Category: Liljas L]] |
| - | [[Category: Tars, K]] | + | [[Category: Plevka P]] |
| - | [[Category: Capsid protein]] | + | [[Category: Tars K]] |
| - | [[Category: Covalent dimer]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Virion]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
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
Particles formed by the bacteriophage MS2 coat protein mutants with insertions in their surface loops induce a strong immune response against the inserted epitopes. The covalent dimers created by fusion of two copies of the coat protein gene are more tolerant to various insertions into the surface loops than the single subunits. We determined a 4.7-A resolution crystal structure of an icosahedral particle assembled from covalent dimers and compared its stability with wild-type virions. The structure resembled the wild-type virion except for the intersubunit linker regions. The covalent dimer orientation was random with respect to both icosahedral twofold and quasi-twofold symmetry axes. A fraction of the particles was unstable in phosphate buffer because of assembly defects. Our results provide a structural background for design of modified covalent coat protein dimer subunits for use in immunization.
Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2.,Plevka P, Tars K, Liljas L Protein Sci. 2009 Aug;18(8):1653-61. PMID:19521994[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
- ↑ Plevka P, Tars K, Liljas L. Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2. Protein Sci. 2009 Aug;18(8):1653-61. PMID:19521994 doi:10.1002/pro.184
|
