6h9c: Difference between revisions
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The | ==Cryo-EM structure of archaeal extremophilic internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) at 3.74 Angstroms resolution.== | ||
<StructureSection load='6h9c' size='340' side='right'caption='[[6h9c]], [[Resolution|resolution]] 3.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6h9c]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Haloarcula_californiae_atcc_33799 Haloarcula californiae atcc 33799]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H9C FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=6h9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9c OCA], [http://pdbe.org/6h9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h9c RCSB], [http://www.ebi.ac.uk/pdbsum/6h9c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9c ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The vertical double beta-barrel major capsid protein (MCP) fold, fingerprint of the PRD1-adeno viral lineage, is widespread in many viruses infecting organisms across the three domains of life. The discovery of PRD1-like viruses with two MCPs challenged the known assembly principles. Here, we present the cryo-electron microscopy (cryo-EM) structures of the archaeal, halophilic, internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) and Haloarcula hispanica icosahedral virus 2 (HHIV-2) at 3.7 and 3.8 A resolution, respectively. Our structures reveal proteins located beneath the morphologically distinct two- and three-tower capsomers and homopentameric membrane proteins at the vertices that orchestrate the positioning of pre-formed vertical single beta-barrel MCP heterodimers. The cryo-EM based structures together with the proteomics data provide insights into the assembly mechanism of this type of viruses and into those with membrane-less double beta-barrel MCPs. | |||
Structural basis for assembly of vertical single beta-barrel viruses.,Santos-Perez I, Charro D, Gil-Carton D, Azkargorta M, Elortza F, Bamford DH, Oksanen HM, Abrescia NGA Nat Commun. 2019 Mar 12;10(1):1184. doi: 10.1038/s41467-019-08927-2. PMID:30862777<ref>PMID:30862777</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6h9c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Haloarcula californiae atcc 33799]] | |||
[[Category: Large Structures]] | |||
[[Category: Abrescia, N G]] | |||
[[Category: Charro, D]] | |||
[[Category: Santos-Perez, I]] | |||
[[Category: Internal membrane-containing archaeal virus]] | |||
[[Category: Vertical single beta-barrel virus]] | |||
[[Category: Virus]] | |||
