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| - | [[Image:1mvb.gif|left|200px]]<br /><applet load="1mvb" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1mvb, resolution 3.0Å" /> | |
| - | '''STRUCTURE OF A PROTEIN CAPSID OF THE T59S MUTANT OF PHAGE MS2'''<br /> | |
| | | | |
| - | ==Overview== | + | ==STRUCTURE OF A PROTEIN CAPSID OF THE T59S MUTANT OF PHAGE MS2== |
| - | In MS2 assembly of phage particles results from an interaction between a, coat protein dimer and a stem-loop of the RNA genome (the operator, hairpin). Amino acid residues Thr45, which is universally conserved among, the small RNA phages, and Thr59 are part of the specific RNA binding, pocket and interact directly with the RNA; the former through a hydrogen, bond, the latter through hydrophobic contacts. The crystal structures of, MS2 protein capsids formed by mutants Thr45Ala and Thr59Ser, both with and, without the 19 nt wild-type operator hairpin bound, are reported here. The, RNA hairpin binds to these mutants in a similar way to its binding to, wild-type protein. In a companion paper both mutants are shown to be, deficient in RNA binding in an in vivo assay, but in vitro the equilibrium, dissociation constant is significantly higher than wild-type for the, Thr45Ala mutant. The change in binding affinity of the Thr45Ala mutant is, probably a direct consequence of removal of direct hydrogen bonds between, the protein and the RNA. The properties of the Thr59Ser mutant are more, difficult to explain, but are consistent with a loss of non-polar contact.
| + | <StructureSection load='1mvb' size='340' side='right'caption='[[1mvb]], [[Resolution|resolution]] 3.00Å' scene=''> |
| - | | + | == Structural highlights == |
| - | ==About this Structure== | + | <table><tr><td colspan='2'>[[1mvb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_MS2 Escherichia phage MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVB FirstGlance]. <br> |
| - | 1MVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacterio_phage_ms2 Enterobacterio phage ms2]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MVB OCA].
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=1mvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvb OCA], [https://pdbe.org/1mvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvb RCSB], [https://www.ebi.ac.uk/pdbsum/1mvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvb ProSAT]</span></td></tr> |
| - | ==Reference== | + | </table> |
| - | Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments., van den Worm SH, Stonehouse NJ, Valegard K, Murray JB, Walton C, Fridborg K, Stockley PG, Liljas L, Nucleic Acids Res. 1998 Mar 1;26(5):1345-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9469847 9469847]
| + | == Function == |
| - | [[Category: Enterobacterio phage ms2]] | + | [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> |
| - | [[Category: Single protein]] | + | == Evolutionary Conservation == |
| - | [[Category: Liljas, L.]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [[Category: Stonehouse, N.J.]] | + | Check<jmol> |
| - | [[Category: Valegard, K.]] | + | <jmolCheckbox> |
| - | [[Category: Vandenworm, S.]] | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mv/1mvb_consurf.spt"</scriptWhenChecked> |
| - | [[Category: bacteriophage coat protein]]
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [[Category: icosahedral virus]]
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | | + | </jmolCheckbox> |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:43:41 2007''
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mvb ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Escherichia phage MS2]] |
| | + | [[Category: Large Structures]] |
| | + | [[Category: Liljas L]] |
| | + | [[Category: Stonehouse NJ]] |
| | + | [[Category: Valegard K]] |
| | + | [[Category: Vandenworm S]] |
| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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
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