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| - | | + | ==Asymmetric structure of a virus-receptor complex== |
| - | <div style="background-color:yellow;" border="1" cellpadding="5">''Warning: this is a large structure, and loading might take a long time or not happen at all.''</div>
| + | <StructureSection load='4bp7' size='340' side='right' caption='[[4bp7]], [[Resolution|resolution]] 39.00Å' scene=''> |
| - | == Asymmetric structure of a virus-receptor complex == | + | |
| - | <StructureSection load='4bp7-pdb-bundle1.pdb.gz' size='340' side='right' caption='[[4bp7]]' scene=''> | + | |
| | == Structural highlights == | | == Structural highlights == |
| - | [[4bp7]] is a 176 chain structure, available for rendering on Proteopedia in 3 parts. | + | <table><tr><td colspan='2'>[[4bp7]] is a 180 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bp6 4bp6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BP7 FirstGlance]. <br> |
| - | You may render each one of these parts individually by selecting here: <jmol><jmolMenu>
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bp4|4bp4]], [[4bp5|4bp5]], [[4bp6|4bp6]]</td></tr> |
| - | <item>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bp7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bp7 RCSB], [http://www.ebi.ac.uk/pdbsum/4bp7 PDBsum]</span></td></tr> |
| - | <script>
| + | </table> |
| - | set echo off; set echo loading 50% 50%; set echo loading center; color echo [xffa500]; background echo translucent 0.7 gray;
| + | == Function == |
| - | echo Loading part 1 ...; refresh;
| + | [[http://www.uniprot.org/uniprot/COAT_BPMS2 COAT_BPMS2]] Forms the phage shell; binds to the phage RNA. |
| - | load models {0 0 1} /cgi-bin/getlateststructure?4bp7-pdb-bundle1.pdb.gz filter "*.CA,*.P|HETATM,![HOH]";
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| - | script /wiki/extensions/Proteopedia/spt/initialview01.spt;
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| - | </script> | + | |
| - | <text>render part 1</text> | + | |
| - | </item> | + | |
| - | <item> | + | |
| - | <script> | + | |
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| - | echo Loading part 2 ...; refresh;
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| - | load models {0 0 1} /cgi-bin/getlateststructure?4bp7-pdb-bundle2.pdb.gz filter "*.CA,*.P|HETATM,![HOH]";
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| - | script /wiki/extensions/Proteopedia/spt/initialview01.spt;
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| - | </script> | + | |
| - | <text>render part 2</text> | + | |
| - | </item> | + | |
| - | <item> | + | |
| - | <script> | + | |
| - | set echo off; set echo loading 50% 50%; set echo loading center; color echo [xffa500]; background echo translucent 0.7 gray;
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| - | echo Loading part 3 ...; refresh;
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| - | load models {0 0 1} /cgi-bin/getlateststructure?4bp7-pdb-bundle3.pdb.gz filter "*.CA,*.P|HETATM,![HOH]";
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| - | script /wiki/extensions/Proteopedia/spt/initialview01.spt;
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| - | </script> | + | |
| - | <text>render part 3</text> | + | |
| - | </item> | + | |
| - | </jmolMenu></jmol>
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| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| - | | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | + | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hiscox, J.A]] | + | [[Category: Enterobacteria phage ms2]] |
| - | [[Category: Dent, K.C]] | + | [[Category: Barker, A M]] |
| - | [[Category: Barker, A.M]] | + | [[Category: Barr, J N]] |
| - | [[Category: Ranson, N.A]] | + | [[Category: Dent, K C]] |
| - | [[Category: Barr, J.N]] | + | [[Category: Hiscox, J A]] |
| - | [[Category: Stockley, P.G]] | + | [[Category: Ranson, N A]] |
| | + | [[Category: Stockley, P G]] |
| | [[Category: Thompson, R]] | | [[Category: Thompson, R]] |
| | + | [[Category: Bacteriophage]] |
| | + | [[Category: Virus]] |
| Structural highlights
Function
[COAT_BPMS2] Forms the phage shell; binds to the phage RNA.
Publication Abstract from PubMed
Simple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and their genomes, which are vital for infection. Here, we report an asymmetric structure of bacteriophage MS2, attached to its receptor, the F-pilus. Cryo-electron tomography and subtomographic averaging of such complexes result in a structure containing clear density for the packaged genome, implying that the conformation of the genome is the same in each virus particle. The data also suggest that the single-copy viral maturation protein breaks the symmetry of the capsid, occupying a position that would be filled by a coat protein dimer in an icosahedral shell. This capsomere can thus fulfill its known biological roles in receptor and genome binding and suggests an exit route for the genome during infection.
The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release.,Dent KC, Thompson R, Barker AM, Hiscox JA, Barr JN, Stockley PG, Ranson NA Structure. 2013 Jun 25. pii: S0969-2126(13)00194-9. doi:, 10.1016/j.str.2013.05.012. PMID:23810697[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dent KC, Thompson R, Barker AM, Hiscox JA, Barr JN, Stockley PG, Ranson NA. The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release. Structure. 2013 Jun 25. pii: S0969-2126(13)00194-9. doi:, 10.1016/j.str.2013.05.012. PMID:23810697 doi:10.1016/j.str.2013.05.012
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