View source for 8aac


==African cichlid nackednavirus capsid at pH 7.5==
<StructureSection load='8aac' size='340' side='right'caption='[[8aac]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8aac]] is a 180 chain structure with sequence from [https://en.wikipedia.org/wiki/African_cichlid_nackednavirus African cichlid nackednavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AAC 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]] 3.7&#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=8aac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aac OCA], [https://pdbe.org/8aac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aac RCSB], [https://www.ebi.ac.uk/pdbsum/8aac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aac ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3S9H6T3_9VIRU A0A3S9H6T3_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The discovery of nackednaviruses provided new insight into the evolutionary history of the hepatitis B virus (HBV): The common ancestor of HBV and nackednaviruses was non-enveloped and while HBV acquired an envelope during evolution, nackednaviruses remained non-enveloped. We report the capsid structure of the African cichlid nackednavirus (ACNDV), determined by cryo-EM at 3.7 A resolution. This enables direct comparison with the known capsid structures of HBV and duck HBV, prototypic representatives of the mammalian and avian lineages of the enveloped Hepadnaviridae, respectively. The sequence identity with HBV is 24% and both the ACNDV capsid protein fold and the capsid architecture are very similar to those of the Hepadnaviridae and HBV in particular. Acquisition of the hepadnaviral envelope was thus not accompanied by a major change in capsid structure. Dynamic residues at the spike tip are tentatively assigned by solid-state NMR, while the C-terminal domain is invisible due to dynamics. Solid-state NMR characterization of the capsid structure reveals few conformational differences between the quasi-equivalent subunits of the ACNDV capsid and an overall higher capsid structural disorder compared to HBV. Despite these differences, the capsids of ACNDV and HBV are structurally highly similar despite the 400 million years since their separation.

Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style.,Pfister S, Rabl J, Wiegand T, Mattei S, Malar AA, Lecoq L, Seitz S, Bartenschlager R, Bockmann A, Nassal M, Boehringer D, Meier BH Nat Commun. 2023 Mar 22;14(1):1574. doi: 10.1038/s41467-023-37068-w. PMID:36949039<ref>PMID:36949039</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8aac" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: African cichlid nackednavirus]]
[[Category: Large Structures]]
[[Category: Boehringer D]]
[[Category: Meier BH]]
[[Category: Pfister S]]
[[Category: Rabl J]]