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6h9c

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'''Unreleased structure'''
 
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The entry 6h9c is ON HOLD until sometime in the future
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==Cryo-EM structure of archaeal extremophilic internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) at 3.74 Angstroms resolution.==
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<SX load='6h9c' size='340' side='right' viewer='molstar' caption='[[6h9c]], [[Resolution|resolution]] 3.74&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6h9c]] is a 32 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=6H9C FirstGlance]. <br>
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</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=6h9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9c OCA], [https://pdbe.org/6h9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h9c RCSB], [https://www.ebi.ac.uk/pdbsum/6h9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A1C7A3R1_9VIRU A0A1C7A3R1_9VIRU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6h9c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Haloarcula californiae ATCC 33799]]
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[[Category: Large Structures]]
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[[Category: Abrescia NG]]
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[[Category: Charro D]]
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[[Category: Santos-Perez I]]

Current revision

Cryo-EM structure of archaeal extremophilic internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) at 3.74 Angstroms resolution.

6h9c, resolution 3.74Å

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