2b2g: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="2b2g" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b2g, resolution 3.02Å" /> '''MS2 Wild-type RNA st...
 
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2b2g.gif|left|200px]]<br /><applet load="2b2g" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2b2g, resolution 3.02&Aring;" />
'''MS2 Wild-type RNA stemloop complexed with an N87S mutant MS2 capsid'''<br />


==Overview==
==MS2 Wild-type RNA stemloop complexed with an N87S mutant MS2 capsid==
Sequence-specific interactions between RNA stem-loops and coat protein, (CP) subunits play vital roles in the life cycles of the RNA, bacteriophages, e.g., by allowing translational repression of their, replicase cistrons and tagging their own RNA genomes for encapsidation., The CPs of bacteriophages Qbeta and MS2 each discriminate in favor of, their cognate translational operators, even in the presence of closely, related operators from other phages in vivo. Discrete mutations within the, MS2 CP have been shown to relax this discrimination in vitro. We have, determined the structures of eight complexes between such mutants and both, MS2 and Qbeta stem-loops with X-ray crystallography. In conjunction with, previously determined in vivo repression data, the structures enable us to, propose the molecular basis for the discrimination mechanism.
<StructureSection load='2b2g' size='340' side='right'caption='[[2b2g]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2b2g]] is a 5 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=2B2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B2G FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.02&#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=2b2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b2g OCA], [https://pdbe.org/2b2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b2g RCSB], [https://www.ebi.ac.uk/pdbsum/2b2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b2g ProSAT]</span></td></tr>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b2/2b2g_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2b2g ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sequence-specific interactions between RNA stem-loops and coat protein (CP) subunits play vital roles in the life cycles of the RNA bacteriophages, e.g., by allowing translational repression of their replicase cistrons and tagging their own RNA genomes for encapsidation. The CPs of bacteriophages Qbeta and MS2 each discriminate in favor of their cognate translational operators, even in the presence of closely related operators from other phages in vivo. Discrete mutations within the MS2 CP have been shown to relax this discrimination in vitro. We have determined the structures of eight complexes between such mutants and both MS2 and Qbeta stem-loops with X-ray crystallography. In conjunction with previously determined in vivo repression data, the structures enable us to propose the molecular basis for the discrimination mechanism.


==About this Structure==
Structural basis of RNA binding discrimination between bacteriophages Qbeta and MS2.,Horn WT, Tars K, Grahn E, Helgstrand C, Baron AJ, Lago H, Adams CJ, Peabody DS, Phillips SE, Stonehouse NJ, Liljas L, Stockley PG Structure. 2006 Mar;14(3):487-95. PMID:16531233<ref>PMID:16531233</ref>
2B2G 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=2B2G OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural basis of RNA binding discrimination between bacteriophages Qbeta and MS2., Horn WT, Tars K, Grahn E, Helgstrand C, Baron AJ, Lago H, Adams CJ, Peabody DS, Phillips SE, Stonehouse NJ, Liljas L, Stockley PG, Structure. 2006 Mar;14(3):487-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16531233 16531233]
</div>
[[Category: Enterobacterio phage ms2]]
<div class="pdbe-citations 2b2g" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Adams, C.J.]]
<references/>
[[Category: Baron, A.J.]]
__TOC__
[[Category: Grahn, E.]]
</StructureSection>
[[Category: Helgstrand, C.]]
[[Category: Escherichia phage MS2]]
[[Category: Horn, W.T.]]
[[Category: Large Structures]]
[[Category: Lago, H.]]
[[Category: Adams CJ]]
[[Category: Liljas, L.]]
[[Category: Baron AJ]]
[[Category: Peabody, D.S.]]
[[Category: Grahn E]]
[[Category: Phillips, S.E.V.]]
[[Category: Helgstrand C]]
[[Category: Stockley, P.G.]]
[[Category: Horn WT]]
[[Category: Stonehouse, N.J.]]
[[Category: Lago H]]
[[Category: Tars, K.]]
[[Category: Liljas L]]
[[Category: capsid]]
[[Category: Peabody DS]]
[[Category: complex (capsid protein - rna hairpin)]]
[[Category: Phillips SEV]]
[[Category: hairpin]]
[[Category: Stockley PG]]
[[Category: levivirus]]
[[Category: Stonehouse NJ]]
[[Category: protein/rna]]
[[Category: Tars K]]
[[Category: virus/viral]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:32:05 2007''

Latest revision as of 11:19, 25 October 2023

MS2 Wild-type RNA stemloop complexed with an N87S mutant MS2 capsidMS2 Wild-type RNA stemloop complexed with an N87S mutant MS2 capsid

Structural highlights

2b2g is a 5 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 3.02Å
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

Sequence-specific interactions between RNA stem-loops and coat protein (CP) subunits play vital roles in the life cycles of the RNA bacteriophages, e.g., by allowing translational repression of their replicase cistrons and tagging their own RNA genomes for encapsidation. The CPs of bacteriophages Qbeta and MS2 each discriminate in favor of their cognate translational operators, even in the presence of closely related operators from other phages in vivo. Discrete mutations within the MS2 CP have been shown to relax this discrimination in vitro. We have determined the structures of eight complexes between such mutants and both MS2 and Qbeta stem-loops with X-ray crystallography. In conjunction with previously determined in vivo repression data, the structures enable us to propose the molecular basis for the discrimination mechanism.

Structural basis of RNA binding discrimination between bacteriophages Qbeta and MS2.,Horn WT, Tars K, Grahn E, Helgstrand C, Baron AJ, Lago H, Adams CJ, Peabody DS, Phillips SE, Stonehouse NJ, Liljas L, Stockley PG Structure. 2006 Mar;14(3):487-95. PMID:16531233[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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
  7. 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

2b2g, resolution 3.02Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA