2bu1

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<StructureSection load='2bu1' size='340' side='right'caption='[[2bu1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2bu1' size='340' side='right'caption='[[2bu1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2bu1]] 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=1e6t 1e6t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BU1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2bu1]] 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=1e6t 1e6t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BU1 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5BU:5-BROMO-URIDINE-5-MONOPHOSPHATE'>5BU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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]], [[1dzs|1dzs]], [[1e7x|1e7x]], [[1gkv|1gkv]], [[1gkw|1gkw]], [[1h8j|1h8j]], [[1hdw|1hdw]], [[1he0|1he0]], [[1he6|1he6]], [[1kuo|1kuo]], [[1msc|1msc]], [[1mst|1mst]], [[1mva|1mva]], [[1mvb|1mvb]], [[1u1y|1u1y]], [[1zdh|1zdh]], [[1zdi|1zdi]], [[1zdj|1zdj]], [[1zdk|1zdk]], [[2bny|2bny]], [[2bq5|2bq5]], [[2bs0|2bs0]], [[2bs1|2bs1]], [[2c4q|2c4q]], [[2c4y|2c4y]], [[2c4z|2c4z]], [[2c50|2c50]], [[2c51|2c51]], [[2ms2|2ms2]], [[5msf|5msf]], [[6msf|6msf]], [[7msf|7msf]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5BU:5-BROMO-URIDINE-5-MONOPHOSPHATE'>5BU</scene></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=2bu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bu1 OCA], [https://pdbe.org/2bu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bu1 RCSB], [https://www.ebi.ac.uk/pdbsum/2bu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bu1 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=2bu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bu1 OCA], [https://pdbe.org/2bu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bu1 RCSB], [https://www.ebi.ac.uk/pdbsum/2bu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bu1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/COAT_BPMS2 COAT_BPMS2]] Forms the phage shell; binds to the phage RNA.
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2bu1 ConSurf].
</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=2bu1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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We have determined the X-ray structures of six MS2 RNA hairpin-coat-protein complexes having five different substitutions at the hairpin loop base -5. This is a uracil in the wild-type hairpin and contacts the coat protein both by stacking on to a tyrosine side chain and by hydrogen bonding to an asparagine side chain. The RNA consensus sequence derived from coat protein binding studies with natural sequence variants suggested that the -5 base needs to be a pyrimidine for strong binding. The five -5 substituents used in this study were 5-bromouracil, pyrimidin-2-one, 2-thiouracil, adenine, and guanine. The structure of the 5-bromouracil complex was determined to 2.2 A resolution, which is the highest to date for any MS2 RNA-protein complex. All the complexes presented here show very similar conformations, despite variation in affinity in solution. The results suggest that the stacking of the -5 base on to the tyrosine side chain is the most important driving force for complex formation. A number of hydrogen bonds that are present in the wild-type complex are not crucial for binding, as they are missing in one or more of the complexes. The results also reveal the flexibility of this RNA-protein interface, with respect to functional group variation, and may be generally applicable to other RNA-protein complexes.
 
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Structural basis of pyrimidine specificity in the MS2 RNA hairpin-coat-protein complex.,Grahn E, Moss T, Helgstrand C, Fridborg K, Sundaram M, Tars K, Lago H, Stonehouse NJ, Davis DR, Stockley PG, Liljas L RNA. 2001 Nov;7(11):1616-27. PMID:11720290<ref>PMID:11720290</ref>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2bu1" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacteriophage ms2]]
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[[Category: Escherichia phage MS2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Davis, D R]]
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[[Category: Davis DR]]
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[[Category: Fridborg, K]]
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[[Category: Fridborg K]]
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[[Category: Grahn, E]]
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[[Category: Grahn E]]
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[[Category: Helgstrand, C]]
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[[Category: Helgstrand C]]
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[[Category: Lago, H]]
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[[Category: Lago H]]
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[[Category: Liljas, L]]
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[[Category: Liljas L]]
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[[Category: Moss, T]]
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[[Category: Moss T]]
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[[Category: Stockley, P G]]
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[[Category: Stockley PG]]
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[[Category: Stonehouse, N J]]
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[[Category: Stonehouse NJ]]
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[[Category: Sundaram, M]]
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[[Category: Sundaram M]]
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[[Category: Tars, K]]
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[[Category: Tars K]]
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[[Category: Capsid]]
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[[Category: Capsid protein]]
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[[Category: Hairpin]]
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[[Category: Icosahedral virus]]
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[[Category: Levivirus]]
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[[Category: Rna-binding]]
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[[Category: Structural protein]]
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[[Category: Virus-rna complex]]
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[[Category: Virus/rna]]
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Current revision

MS2-RNA HAIRPIN (5BRU -5) COMPLEX

PDB ID 2bu1

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