1qbe

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{{Seed}}
 
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[[Image:1qbe.png|left|200px]]
 
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==BACTERIOPHAGE Q BETA CAPSID==
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The line below this paragraph, containing "STRUCTURE_1qbe", creates the "Structure Box" on the page.
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<StructureSection load='1qbe' size='340' side='right'caption='[[1qbe]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qbe]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Qbeta Escherichia virus Qbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QBE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 3.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qbe OCA], [https://pdbe.org/1qbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qbe RCSB], [https://www.ebi.ac.uk/pdbsum/1qbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qbe ProSAT]</span></td></tr>
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{{STRUCTURE_1qbe| PDB=1qbe | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAPSD_BPQBE CAPSD_BPQBE] Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:27671640, PubMed:19913556). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:8943226, PubMed:27671640). Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556). The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640).<ref>PMID:19913556</ref> <ref>PMID:27671640</ref> <ref>PMID:8943226</ref> Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.<ref>PMID:8943226</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qb/1qbe_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1qbe ConSurf].
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<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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BACKGROUND: The capsid protein subunits of small RNA bacteriophages form a T = 3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this interaction is believed to initiate RNA encapsidation. We have determined the crystal structure of phage Q beta with the aim of clarifying which factors are the most important for particle assembly and RNA interaction in the small phages. RESULTS: The crystal structure of bacteriophage Q beta determined at 3.5 A resolution shows that the capsid is stabilized by disulfide bonds on each side of the flexible loops that are situated around the fivefold and quasi-sixfold axes. As in other small RNA phages, the protein capsid is constructed from subunits which associate into dimers. A contiguous ten-stranded antiparallel beta sheet facing the RNA is formed in the dimer. The disulfide bonds lock the constituent dimers of the capsid covalently in the T = 3 lattice. CONCLUSIONS: The unusual stability of the Q beta particle is due to the tight dimer interactions and the disulfide bonds linking each dimer covalently to the rest of the capsid. A comparison with the structure of the related phage MS2 shows that although the fold of the Q beta coat protein is very similar, the details of the protein-protein interactions are completely different. The most conserved region of the protein is at the surface, which, in MS2, is involved in RNA binding.
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===BACTERIOPHAGE Q BETA CAPSID===
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The crystal structure of bacteriophage Q beta at 3.5 A resolution.,Golmohammadi R, Fridborg K, Bundule M, Valegard K, Liljas L Structure. 1996 May 15;4(5):543-54. PMID:8736553<ref>PMID:8736553</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_8736553}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qbe" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 8736553 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8736553}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia virus Qbeta]]
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1QBE is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_qbeta Enterobacteria phage qbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QBE OCA].
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[[Category: Large Structures]]
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[[Category: Golmohammadi R]]
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==Reference==
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[[Category: Liljas L]]
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<ref group="xtra">PMID:8736553</ref><references group="xtra"/>
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[[Category: Enterobacteria phage qbeta]]
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[[Category: Golmohammadi, R.]]
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[[Category: Liljas, L.]]
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[[Category: Coat protein]]
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[[Category: Icosahedral virus]]
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[[Category: Rna binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:47:14 2009''
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Current revision

BACTERIOPHAGE Q BETA CAPSID

PDB ID 1qbe

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