6QI5 image
Deposition Date 2019-01-17
Release Date 2020-08-05
Last Version Date 2024-05-15
Entry Detail
PDB ID:
6QI5
Keywords:
Title:
Near Atomic Structure of an Atadenovirus Shows a possible gene duplication event and Intergenera Variations in Cementing Proteins
Biological Source:
Source Organism(s):
Method Details:
Experimental Method:
Resolution:
3.40 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Hexon protein
Chain IDs:A, B (auth: L), C (auth: K), D (auth: J), E (auth: H), F (auth: I), G, H (auth: F), I (auth: E), J (auth: D), K (auth: C), L (auth: B)
Chain Length:909
Number of Molecules:12
Biological Source:Lizard adenovirus 2
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Penton protein
Gene (Uniprot):L2
Chain IDs:T (auth: M)
Chain Length:451
Number of Molecules:1
Biological Source:Lizard adenovirus 2
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:PIIIa
Chain IDs:S (auth: N)
Chain Length:609
Number of Molecules:1
Biological Source:Lizard adenovirus 2
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Pre-hexon-linking protein VII
Gene (Uniprot):L4
Chain IDs:Q (auth: P), R (auth: O)
Chain Length:278
Number of Molecules:2
Biological Source:Lizard adenovirus 2
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Protein LH3
Chain IDs:M (auth: S), N (auth: T), O (auth: R), P (auth: Q)
Chain Length:370
Number of Molecules:4
Biological Source:Lizard adenovirus 2
Ligand Molecules
Primary Citation
Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins.
Sci Adv 7 ? ? (2021)
PMID: 33789897 DOI: 10.1126/sciadv.abe6008

Abstact

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.

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Chemical

Disease

Primary Citation of related structures
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