View source for 5oxe


==Structure of major capsid protein VP1 of Aeropyrum pernix bacilliform virus 1 APBV1==
<SX load='5oxe' size='340' side='right' viewer='molstar' caption='[[5oxe]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5oxe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_bacilliform_virus_1_Japan/Tanaka/2005 Aeropyrum pernix bacilliform virus 1 Japan/Tanaka/2005]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OXE 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]] 3.5&#8491;</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=5oxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oxe OCA], [https://pdbe.org/5oxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oxe RCSB], [https://www.ebi.ac.uk/pdbsum/5oxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oxe ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/D4QF72_APBV1 D4QF72_APBV1] 
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== Publication Abstract from PubMed ==
Archaeal viruses have evolved to infect hosts often thriving in extreme conditions such as high temperatures. However, there is a paucity of information on archaeal virion structures, genome packaging, and determinants of temperature resistance. The rod-shaped virus APBV1 (Aeropyrum pernix bacilliform virus 1) is among the most thermostable viruses known; it infects a hyperthermophile Aeropyrum pernix, which grows optimally at 90 degrees C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. Tight packing of the major virion glycoprotein (VP1) is ensured by extended hydrophobic interfaces, and likely contributes to the extreme thermostability of the helical capsid. The double-stranded DNA is tightly packed in the capsid as a left-handed superhelix and held in place by the interactions with positively charged residues of VP1. The assembly is closed by specific capping structures at either end, which we propose to play a role in DNA packing and delivery.

Unique architecture of thermophilic archaeal virus APBV1 and its genome packaging.,Ptchelkine D, Gillum A, Mochizuki T, Lucas-Staat S, Liu Y, Krupovic M, Phillips SEV, Prangishvili D, Huiskonen JT Nat Commun. 2017 Nov 10;8(1):1436. doi: 10.1038/s41467-017-01668-0. PMID:29127347<ref>PMID:29127347</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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[[Category: Aeropyrum pernix bacilliform virus 1 Japan/Tanaka/2005]]
[[Category: Large Structures]]
[[Category: Huiskonen JT]]
[[Category: Phillpps SEV]]
[[Category: Ptchelkine D]]