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6QI5

Near Atomic Structure of an Atadenovirus Shows a possible gene duplication event and Intergenera Variations in Cementing Proteins

This is a non-PDB format compatible entry.
Summary for 6QI5
Entry DOI10.2210/pdb6qi5/pdb
EMDB information4551
DescriptorHexon protein, Protein LH3, Pre-hexon-linking protein VIII, ... (5 entities in total)
Functional Keywordsadenovirus atadenovirus virus evolution, virus
Biological sourceLizard adenovirus 2
More
Total number of polymer chains20
Total formula weight1566134.56
Authors
Condezo, G.N.,Marabini, R.,Gomez-Blanco, J.,SanMartin, C. (deposition date: 2019-01-17, release date: 2020-08-05, Last modification date: 2024-05-15)
Primary citationMarabini, R.,Condezo, G.N.,Krupovic, M.,Menendez-Conejero, R.,Gomez-Blanco, J.,San Martin, C.
Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins.
Sci Adv, 7:-, 2021
Cited by
PubMed Abstract: Of five known adenovirus genera, high-resolution structures are available only for mammalian-infecting mastadenoviruses. We present the first high-resolution structure of an adenovirus with nonmammalian host: lizard atadenovirus LAdV-2. We find a large conformational difference in the internal vertex protein IIIa between mast- and atadenoviruses, induced by the presence of an extended polypeptide. This polypeptide, and α-helical clusters beneath the facet, likely correspond to genus-specific proteins LH2 and p32k. Another genus-specific protein, LH3, with a fold typical of bacteriophage tailspikes, contacts the capsid surface via a triskelion structure identical to that used by mastadenovirus protein IX, revealing a conserved capsid-binding motif and an ancient gene duplication event. Our data also suggest that mastadenovirus E1B-55 K was exapted from the atadenovirus-like LH3 protein. This work provides new information on the evolution of adenoviruses, emphasizing the importance of minor coat proteins for determining specific physicochemical properties of virions and most likely their tropism.
PubMed: 33789897
DOI: 10.1126/sciadv.abe6008
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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