6hm8

Crystal structure of human ACBD3 GOLD domain in complex with 3A protein of enterovirus-D68 (fusion protein)

spinqualitylabelsall models 6hm8, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hm8 is a 2 chain structure with sequence from Homo sapiens and Enterovirus D68. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.277Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GCP60_HUMAN Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity). Publication Abstract from PubMed Enteroviruses, members of the family of picornaviruses, are the most common viral infectious agents in humans causing a broad spectrum of diseases ranging from mild respiratory illnesses to life-threatening infections. To efficiently replicate within the host cell, enteroviruses hijack several host factors, such as ACBD3. ACBD3 facilitates replication of various enterovirus species, however, structural determinants of ACBD3 recruitment to the viral replication sites are poorly understood. Here, we present a structural characterization of the interaction between ACBD3 and the non-structural 3A proteins of four representative enteroviruses (poliovirus, enterovirus A71, enterovirus D68, and rhinovirus B14). In addition, we describe the details of the 3A-3A interaction causing the assembly of the ACBD3-3A heterotetramers and the interaction between the ACBD3-3A complex and the lipid bilayer. Using structure-guided identification of the point mutations disrupting these interactions, we demonstrate their roles in the intracellular localization of these proteins, recruitment of downstream effectors of ACBD3, and facilitation of enterovirus replication. These structures uncovered a striking convergence in the mechanisms of how enteroviruses and kobuviruses, members of a distinct group of picornaviruses that also rely on ACBD3, recruit ACBD3 and its downstream effectors to the sites of viral replication. Convergent evolution in the mechanisms of ACBD3 recruitment to picornavirus replication sites.,Horova V, Lyoo H, Rozycki B, Chalupska D, Smola M, Humpolickova J, Strating JRPM, van Kuppeveld FJM, Boura E, Klima M PLoS Pathog. 2019 Aug 5;15(8):e1007962. doi: 10.1371/journal.ppat.1007962. PMID:31381608 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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