8fqk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Asymmetric unit of HK97 phage prohead I== | |
| + | <StructureSection load='8fqk' size='340' side='right'caption='[[8fqk]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8fqk]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_HK97 Escherichia phage HK97]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FQK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fqk OCA], [https://pdbe.org/8fqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fqk RCSB], [https://www.ebi.ac.uk/pdbsum/8fqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fqk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAPSD_BPHK7 CAPSD_BPHK7] Assembles to form an icosahedral capsid of 66 nm, with a T=7 laevo symmetry (PubMed:11000116, PubMed:21276801). Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function.<ref>PMID:11000116</ref> <ref>PMID:21276801</ref> <ref>PMID:7669350</ref> <ref>PMID:7723020</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tailed bacteriophages and herpesviruses use a transient scaffold to assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold portal is thought to nucleate the assembly. How does the scaffold orchestrate this step? We have determined the portal vertex structure of the bacteriophage HK97 procapsid, where the scaffold is a domain of the major capsid protein. The scaffold forms rigid helix-turn-strand structures on the interior surfaces of all capsomers and is further stabilized around the portal, forming trimeric coiled-coil towers, two per surrounding capsomer. These 10 towers bind identically to 10 of 12 portal subunits, adopting a pseudo-12-fold organization that explains how the symmetry mismatch is managed at this early step. | ||
| - | + | A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex.,Huet A, Oh B, Maurer J, Duda RL, Conway JF Sci Adv. 2023 Jun 16;9(24):eadg8868. doi: 10.1126/sciadv.adg8868. Epub 2023 Jun , 16. PMID:37327331<ref>PMID:37327331</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8fqk" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Duda | + | <references/> |
| - | [[Category: Huet | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Escherichia phage HK97]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Conway JF]] | ||
| + | [[Category: Duda RL]] | ||
| + | [[Category: Huet A]] | ||
| + | [[Category: Maurer J]] | ||
| + | [[Category: Oh B]] | ||
Revision as of 21:18, 28 June 2023
Asymmetric unit of HK97 phage prohead I
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