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5LZ1

Crystal structure of human ACBD3 GOLD domain

Summary for 5LZ1
Entry DOI10.2210/pdb5lz1/pdb
DescriptorGolgi resident protein GCP60 (2 entities in total)
Functional Keywordsacbd3, gold, signaling protein
Biological sourceHomo sapiens (Human)
Cellular locationGolgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9H3P7
Total number of polymer chains1
Total formula weight19389.35
Authors
Klima, M.,Boura, E. (deposition date: 2016-09-29, release date: 2016-12-14, Last modification date: 2024-01-17)
Primary citationKlima, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

건을2024-10-30부터공개중

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