5LZ3

Crystal structure of human ACBD3 GOLD domain in complex with 3A protein of Aichivirus A

Summary for 5LZ3

• Entry DOI: 10.2210/pdb5lz3/pdb
• Descriptor: Golgi resident protein GCP60, 3A (2 entities in total)
• Functional Keywords: acbd3, gold, 3a, aichivirus, antiviral protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9H3P7; Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : O91464
• Total number of polymer chains: 2
• Total formula weight: 25873.68

Authors

Klima, M.,Boura, E. (deposition date: 2016-09-29, release date: 2016-12-14, Last modification date: 2024-01-17)

Primary citation

Klima, M.,Chalupska, D.,Rozycki, B.,Humpolickova, J.,Rezabkova, L.,Silhan, J.,Baumlova, A.,Dubankova, A.,Boura, E.
Kobuviral Non-structural 3A Proteins Act as Molecular Harnesses to Hijack the Host ACBD3 Protein.
Structure, 25:219-230, 2017

PubMed Abstract: Picornaviruses are small positive-sense single-stranded RNA viruses that include many important human pathogens. Within the host cell, they replicate at specific replication sites called replication organelles. To create this membrane platform, they hijack several host factors including the acyl-CoA-binding domain-containing protein-3 (ACBD3). Here, we present a structural characterization of the molecular complexes formed by the non-structural 3A proteins from two species of the Kobuvirus genus of the Picornaviridae family and the 3A-binding domain of the host ACBD3 protein. Specifically, we present a series of crystal structures as well as a molecular dynamics simulation of the 3A:ACBD3 complex at the membrane, which reveals that the viral 3A proteins act as molecular harnesses to enslave the ACBD3 protein leading to its stabilization at target membranes. Our data provide a structural rationale for understanding how these viral-host protein complexes assemble at the atomic level and identify new potential targets for antiviral therapies.

PubMed: 28065508
DOI: 10.1016/j.str.2016.11.021

Experimental method

X-RAY DIFFRACTION (3 Å)