5vlz

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{{Large structure}}
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==Backbone model for phage Qbeta capsid==
==Backbone model for phage Qbeta capsid==
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<StructureSection load='5vlz' size='340' side='right' caption='[[5vlz]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
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<StructureSection load='5vlz' size='340' side='right'caption='[[5vlz]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5vlz]] is a 181 chain structure with sequence from [http://en.wikipedia.org/wiki/Allolevivirus_subgroup_iii Allolevivirus subgroup iii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VLZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[5vlz]] is a 181 chain structure with sequence from [http://en.wikipedia.org/wiki/Allolevivirus_subgroup_iii Allolevivirus subgroup iii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VLZ FirstGlance]. <br>
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<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=5vlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vlz OCA], [http://pdbe.org/5vlz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vlz RCSB], [http://www.ebi.ac.uk/pdbsum/5vlz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vlz ProSAT]</span></td></tr>
<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=5vlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vlz OCA], [http://pdbe.org/5vlz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vlz RCSB], [http://www.ebi.ac.uk/pdbsum/5vlz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vlz ProSAT]</span></td></tr>
</table>
</table>
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{{Large structure}}
 
== Function ==
== Function ==
[[http://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> [[http://www.uniprot.org/uniprot/MATA2_BPQBE MATA2_BPQBE]] Induces host cell lysis (PubMed:11892805). Inhibits host MurA activity thereby blocking the synthesis of murein precursors necessary for the host cell wall biosynthesis (PubMed:11423662). May be responsible for the attachment to the host pilus. Makes extensive contacts with the viral genome (PubMed:28111107).<ref>PMID:11423662</ref> <ref>PMID:11892805</ref> <ref>PMID:23329676</ref> <ref>PMID:28111107</ref>
[[http://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> [[http://www.uniprot.org/uniprot/MATA2_BPQBE MATA2_BPQBE]] Induces host cell lysis (PubMed:11892805). Inhibits host MurA activity thereby blocking the synthesis of murein precursors necessary for the host cell wall biosynthesis (PubMed:11423662). May be responsible for the attachment to the host pilus. Makes extensive contacts with the viral genome (PubMed:28111107).<ref>PMID:11423662</ref> <ref>PMID:11892805</ref> <ref>PMID:23329676</ref> <ref>PMID:28111107</ref>
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</StructureSection>
</StructureSection>
[[Category: Allolevivirus subgroup iii]]
[[Category: Allolevivirus subgroup iii]]
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[[Category: Large Structures]]
[[Category: Cui, Z]]
[[Category: Cui, Z]]
[[Category: Zhang, J]]
[[Category: Zhang, J]]

Revision as of 09:09, 18 December 2019

Backbone model for phage Qbeta capsid

PDB ID 5vlz

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