|
|
| (6 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==In situ structures of the genome and genome-delivery apparatus in ssRNA bacteriophage MS2== | | ==In situ structures of the genome and genome-delivery apparatus in ssRNA bacteriophage MS2== |
| - | <StructureSection load='5tc1' size='340' side='right' caption='[[5tc1]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2] and [http://en.wikipedia.org/wiki/Enterobacterio_phage_ms2 Enterobacterio phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TC1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tc1]] is a 10 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=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TC1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ms2|2ms2]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</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=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [http://pdbe.org/5tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</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=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [https://pdbe.org/5tc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [https://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> [[http://www.uniprot.org/uniprot/MAT_BPMS2 MAT_BPMS2]] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). MP binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-MP complex is released from the capsid upon host receptor binding (PubMed:23810697). MP enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref> | + | [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> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Enterobacteria phage ms2]] | + | [[Category: Escherichia virus MS2]] |
| - | [[Category: Enterobacterio phage ms2]] | + | [[Category: Large Structures]] |
| - | [[Category: Dai, X H]] | + | [[Category: Dai XH]] |
| - | [[Category: Du, Y S]] | + | [[Category: Du YS]] |
| - | [[Category: Lai, M]] | + | [[Category: Lai M]] |
| - | [[Category: Li, Z H]] | + | [[Category: Li ZH]] |
| - | [[Category: Shu, S]] | + | [[Category: Shu S]] |
| - | [[Category: Sun, R]] | + | [[Category: Sun R]] |
| - | [[Category: Zhou, Z H]] | + | [[Category: Zhou ZH]] |
| - | [[Category: Asymmetric cryoem reconstruction]]
| + | |
| - | [[Category: Genome-capsid interaction]]
| + | |
| - | [[Category: Genome-delivery apparatus]]
| + | |
| - | [[Category: Ssrna genome structure]]
| + | |
| - | [[Category: Viral protein-rna complex]]
| + | |
| 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]
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
|