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2izm

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Revision as of 12:49, 22 February 2023

MS2-RNA HAIRPIN (C-10) COMPLEX

Structural highlights

2izm is a 5 chain structure with sequence from Escherichia phage MS2. This structure supersedes the now removed PDB entry 1kuo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We have determined the structures of complexes between the phage MS2 coat protein and variants of the replicase translational operator in order to explore the sequence specificity of the RNA-protein interaction. The 19-nt RNA hairpins studied have substitutions at two positions that have been shown to be important for specific binding. At one of these positions, -10, which is a bulged adenosine (A) in the stem of the wild-type operator hairpin, substitutions were made with guanosine (G), cytidine (C) and two non-native bases, 2-aminopurine (2AP) and inosine (I). At the other position, -7 in the hairpin loop, the native adenine was substituted with a cytidine. Of these, only the G-10, C-10 and C-7 variants showed interpretable density for the RNA hairpin. In spite of large differences in binding affinities, the structures of the variant complexes are very similar to the wild-type operator complex. For G-10 substitutions in hairpin variants that can form bulges at alternative places in the stem, the binding affinity is low and a partly disordered conformation is seen in the electron density maps. The affinity is similar to that of wild-type when the base pairs adjacent to the bulged nucleotide are selected to avoid alternative conformations. Both purines bind in a very similar way in a pocket in the protein. In the C-10 variant, which has very low affinity, the cytidine is partly inserted in the protein pocket rather than intercalated in the RNA stem. Substitution of the wild-type adenosine at position -7 by pyrimidines gives strongly reduced affinities, but the structure of the C-7 complex shows that the base occupies the same position as the A-7 in the wild-type RNA. It is stacked in the RNA and makes no direct contact with the protein.

Investigating the structural basis of purine specificity in the structures of MS2 coat protein RNA translational operator hairpins.,Helgstrand C, Grahn E, Moss T, Stonehouse NJ, Tars K, Stockley PG, Liljas L Nucleic Acids Res. 2002 Jun 15;30(12):2678-85. PMID:12060685^[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
↑ Helgstrand C, Grahn E, Moss T, Stonehouse NJ, Tars K, Stockley PG, Liljas L. Investigating the structural basis of purine specificity in the structures of MS2 coat protein RNA translational operator hairpins. Nucleic Acids Res. 2002 Jun 15;30(12):2678-85. PMID:12060685

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2izm"

@@ Line 3: / Line 3: @@
 <StructureSection load='2izm' size='340' side='right'caption='[[2izm]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2izm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_ms2 Bacteriophage ms2]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kuo 1kuo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IZM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2izm]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_MS2 Escherichia phage MS2]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kuo 1kuo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IZM FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aq3|1aq3]], [[1aq4|1aq4]], [[1bms|1bms]], [[1msc|1msc]], [[1mst|1mst]], [[1mva|1mva]], [[1mvb|1mvb]], [[1u1y|1u1y]], [[1zdh|1zdh]], [[1zdi|1zdi]], [[1zdj|1zdj]], [[1zdk|1zdk]], [[1zse|1zse]], [[2b2d|2b2d]], [[2b2e|2b2e]], [[2b2g|2b2g]], [[2bny|2bny]], [[2bq5|2bq5]], [[2bs0|2bs0]], [[2bs1|2bs1]], [[2bu1|2bu1]], [[2c4q|2c4q]], [[2c4y|2c4y]], [[2c4z|2c4z]], [[2c50|2c50]], [[2c51|2c51]], [[2ms2|2ms2]], [[5msf|5msf]], [[6msf|6msf]], [[7msf|7msf]], [[2iz8|2iz8]], [[2iz9|2iz9]], [[2izn|2izn]]</div></td></tr>
+</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=2izm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izm OCA], [https://pdbe.org/2izm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2izm RCSB], [https://www.ebi.ac.uk/pdbsum/2izm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2izm 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=2izm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izm OCA], [https://pdbe.org/2izm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2izm RCSB], [https://www.ebi.ac.uk/pdbsum/2izm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2izm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: Bacteriophage ms2]]
+[[Category: Escherichia phage MS2]]
 [[Category: Large Structures]]
-[[Category: Grahn, E]]
+[[Category: Grahn E]]
-[[Category: Helgstrand, C]]
+[[Category: Helgstrand C]]
-[[Category: Liljas, L]]
+[[Category: Liljas L]]
-[[Category: Moss, T]]
+[[Category: Moss T]]
-[[Category: Stockley, P G]]
+[[Category: Stockley PG]]
-[[Category: Stonehouse, N J]]
+[[Category: Stonehouse NJ]]
-[[Category: Tars, K]]
+[[Category: Tars K]]
-[[Category: Capsid]]
-[[Category: Capsid protein]]
-[[Category: Hairpin]]
-[[Category: Levivirus]]
-[[Category: Rna-binding]]
-[[Category: Structural protein]]
-[[Category: Virion protein]]
-[[Category: Virus-rna complex]]
-[[Category: Virus/rna]]
-[[Category: Virus/viral protein/rna]]

2izm

From Proteopedia

Revision as of 12:49, 22 February 2023

MS2-RNA HAIRPIN (C-10) COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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