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6qjt

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<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution|resolution]] 3.74&Aring;' scene=''>
<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution|resolution]] 3.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QJT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QJT FirstGlance]. <br>
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</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=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [http://pdbe.org/6qjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [http://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [http://pdbe.org/6qjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [http://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]
[[http://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The portal protein is a key component of many double-stranded DNA viruses, governing capsid assembly and genome packaging. Twelve subunits of the portal protein define a tunnel, through which DNA is translocated into the capsid. It is unknown how the portal protein functions as a gatekeeper, preventing DNA slippage, whilst allowing its passage into the capsid, and how these processes are controlled. A cryo-EM structure of the portal protein of thermostable virus P23-45, determined in situ in its procapsid-bound state, indicates a mechanism that naturally safeguards the virus against genome loss. This occurs via an inversion of the conformation of the loops that define the constriction in the central tunnel, accompanied by a hydrophilic-hydrophobic switch. The structure also shows how translocation of DNA into the capsid could be modulated by a changing mode of protein-protein interactions between portal and capsid, across a symmetry-mismatched interface.
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Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss.,Bayfield OW, Steven AC, Antson AA Elife. 2020 Apr 14;9. pii: 55517. doi: 10.7554/eLife.55517. PMID:32286226<ref>PMID:32286226</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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</div>
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<div class="pdbe-citations 6qjt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 06:04, 22 April 2020

Thermophage P23-45 in situ procapsid portal protein

PDB ID 6qjt

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