5jj1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Immature Procapsid Conformation of P22 Portal Protein== | |
| + | <StructureSection load='5jj1' size='340' side='right' caption='[[5jj1]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jj1]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JJ1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v4k|4v4k]], [[3lj4|3lj4]], [[3lj5|3lj5]], [[5jj3|5jj3]]</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=5jj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jj1 OCA], [http://pdbe.org/5jj1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jj1 RCSB], [http://www.ebi.ac.uk/pdbsum/5jj1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jj1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PORTL_BPP22 PORTL_BPP22]] Required for successful condensation of DNA within the capsid. Gp1 is a minor structural protein. The portal protein is present as a single ring-shaped dodecamer located at the point where tails attach. It is through this ring that DNA is thought to enter the prohead. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tailed bacteriophages and herpesviruses assemble infectious particles via an empty precursor capsid (or 'procapsid') built by multiple copies of coat and scaffolding protein and by one dodecameric portal protein. Genome packaging triggers rearrangement of the coat protein and release of scaffolding protein, resulting in dramatic procapsid lattice expansion. Here, we provide structural evidence that the portal protein of the bacteriophage P22 exists in two distinct dodecameric conformations: an asymmetric assembly in the procapsid (PC-portal) that is competent for high affinity binding to the large terminase packaging protein, and a symmetric ring in the mature virion (MV-portal) that has negligible affinity for the packaging motor. Modelling studies indicate the structure of PC-portal is incompatible with DNA coaxially spooled around the portal vertex, suggesting that newly packaged DNA triggers the switch from PC- to MV-conformation. Thus, we propose the signal for termination of 'Headful Packaging' is a DNA-dependent symmetrization of portal protein. | ||
| - | + | Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation.,Lokareddy RK, Sankhala RS, Roy A, Afonine PV, Motwani T, Teschke CM, Parent KN, Cingolani G Nat Commun. 2017 Jan 30;8:14310. doi: 10.1038/ncomms14310. PMID:28134243<ref>PMID:28134243</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5jj1" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Cingolani, G]] | [[Category: Cingolani, G]] | ||
| + | [[Category: Lokareddy, R K]] | ||
| + | [[Category: Dodecamer]] | ||
| + | [[Category: Packaging motor]] | ||
| + | [[Category: Portal protein]] | ||
| + | [[Category: Procapsid]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 08:29, 9 March 2017
Structure of the Immature Procapsid Conformation of P22 Portal Protein
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