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| | ==Asymmetric unit for the coat proteins of phage Qbeta== | | ==Asymmetric unit for the coat proteins of phage Qbeta== |
| - | <StructureSection load='5vly' size='340' side='right' caption='[[5vly]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <SX load='5vly' size='340' side='right' viewer='molstar' caption='[[5vly]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vly]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_phage_qbeta Escherichia phage qbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VLY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VLY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vly]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Qbeta Escherichia virus Qbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VLY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vlz|5vlz]], [[5vm7|5vm7]]</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]] 3.3Å</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=5vly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vly OCA], [http://pdbe.org/5vly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vly RCSB], [http://www.ebi.ac.uk/pdbsum/5vly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vly 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=5vly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vly OCA], [https://pdbe.org/5vly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vly RCSB], [https://www.ebi.ac.uk/pdbsum/5vly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vly ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAPSD_BPQBE CAPSD_BPQBE]] Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:27671640, PubMed:19913556). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:8943226, PubMed:27671640). Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556). The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640).<ref>PMID:19913556</ref> <ref>PMID:27671640</ref> <ref>PMID:8943226</ref> Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.<ref>PMID:8943226</ref> | + | [https://www.uniprot.org/uniprot/CAPSD_BPQBE CAPSD_BPQBE] Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:27671640, PubMed:19913556). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:8943226, PubMed:27671640). Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556). The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640).<ref>PMID:19913556</ref> <ref>PMID:27671640</ref> <ref>PMID:8943226</ref> Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.<ref>PMID:8943226</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Escherichia phage qbeta]] | + | [[Category: Escherichia virus Qbeta]] |
| - | [[Category: Cui, Z]] | + | [[Category: Large Structures]] |
| - | [[Category: Zhang, J]] | + | [[Category: Cui Z]] |
| - | [[Category: Phage]] | + | [[Category: Zhang J]] |
| - | [[Category: Qbeta]]
| + | |
| - | [[Category: Ssrna]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
CAPSD_BPQBE Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:27671640, PubMed:19913556). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:8943226, PubMed:27671640). Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556). The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640).[1] [2] [3] Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.[4]
References
- ↑ Basnak G, Morton VL, Rolfsson O, Stonehouse NJ, Ashcroft AE, Stockley PG. Viral genomic single-stranded RNA directs the pathway toward a T=3 capsid. J Mol Biol. 2010 Feb 5;395(5):924-36. doi: 10.1016/j.jmb.2009.11.018. Epub 2009, Nov 12. PMID:19913556 doi:http://dx.doi.org/10.1016/j.jmb.2009.11.018
- ↑ Gorzelnik KV, Cui Z, Reed CA, Jakana J, Young R, Zhang J. Asymmetric cryo-EM structure of the canonical Allolevivirus Qbeta reveals a single maturation protein and the genomic ssRNA in situ. Proc Natl Acad Sci U S A. 2016 Sep 26. pii: 201609482. PMID:27671640 doi:http://dx.doi.org/10.1073/pnas.1609482113
- ↑ Lim F, Spingola M, Peabody DS. The RNA-binding site of bacteriophage Qbeta coat protein. J Biol Chem. 1996 Dec 13;271(50):31839-45. PMID:8943226
- ↑ Lim F, Spingola M, Peabody DS. The RNA-binding site of bacteriophage Qbeta coat protein. J Biol Chem. 1996 Dec 13;271(50):31839-45. PMID:8943226
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