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2vtu

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crystal structure of bacteriophage MS2 covalent coat protein dimer

Structural highlights

2vtu is a 2 chain structure with sequence from Escherichia phage MS2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.5Å
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]

Publication Abstract from PubMed

A covalent dimer of the bacteriophage MS2 coat protein was created by performing genetic fusion of two copies of the gene while removing the stop codon of the first gene. The dimer was crystallized in the cubic F432 space group. The organization of the asymmetric unit together with the F432 symmetry results in an arrangement of subunits that corresponds to T = 3 octahedral particles. The octahedral particles are probably artifacts created by the particular crystal packing. When it is not crystallized in the F cubic crystal form, the coat protein dimer appears to assemble into T = 3 icosahedral particles indistinguishable from the wild-type particles. To form an octahedral particle with closed surface, the dimer subunits interact at sharper angles than in the icosahedral arrangement. The fold of the covalent dimer is almost identical to the wild-type dimer with differences located in loops and in the covalent linker region. The main differences in the subunit packing between the octahedral and icosahedral arrangements are located close to the fourfold and fivefold symmetry axes where different sets of loops mediate the contacts. The volume of the wild-type virions is 7 times bigger than that of the octahedral particles.

Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles.,Plevka P, Tars K, Liljas L Protein Sci. 2008 Oct;17(10):1731-9. Epub 2008 Jul 28. PMID:18662904^[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. 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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Escherichia phage MS2 | Large Structures | Liljas L | Plevka P | Tars K

@@ Line 3: / Line 3: @@
 <StructureSection load='2vtu' size='340' side='right'caption='[[2vtu]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vtu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_ms2 Bacteriophage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VTU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vtu]] is a 2 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=2VTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VTU 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;'>[[2b2e|2b2e]], [[6msf|6msf]], [[2bs0|2bs0]], [[7msf|7msf]], [[2iz9|2iz9]], [[2b2g|2b2g]], [[2c4q|2c4q]], [[2c4y|2c4y]], [[1zdj|1zdj]], [[2c4z|2c4z]], [[2c51|2c51]], [[2bny|2bny]], [[1u1y|1u1y]], [[1mvb|1mvb]], [[2bs1|2bs1]], [[1msc|1msc]], [[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]], [[2bu1|2bu1]], [[2izm|2izm]]</div></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]] 3.5&#8491;</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=2vtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vtu OCA], [https://pdbe.org/2vtu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vtu RCSB], [https://www.ebi.ac.uk/pdbsum/2vtu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vtu 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacteriophage ms2]]
+[[Category: Escherichia phage MS2]]
 [[Category: Large Structures]]
-[[Category: Liljas, L]]
+[[Category: Liljas L]]
-[[Category: Plevka, P]]
+[[Category: Plevka P]]
-[[Category: Tars, K]]
+[[Category: Tars K]]
-[[Category: Capsid protein]]
-[[Category: Coat protein]]
-[[Category: Dimer]]
-[[Category: Ms2]]
-[[Category: Octahedron]]
-[[Category: Rna-binding]]
-[[Category: Virion]]
-[[Category: Virus]]

2vtu

From Proteopedia

Current revision

crystal structure of bacteriophage MS2 covalent coat protein dimer

Structural highlights

Function

Publication Abstract from PubMed

References

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