9iw0 | pdb_00009iw0

Structure of Adenovirus serotype 3 mature hexon

spinqualitylabelsall models 9iw0, resolution 3.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9iw0 is a 3 chain structure with sequence from Human adenovirus B3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.24Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2Y0H4_ADE03 Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.[ARBA:ARBA00024662][HAMAP-Rule:MF_04051] Publication Abstract from PubMed Adenovirus is an icosahedral, non-enveloped DNA virus that infects humans and other animals. The capsid of adenovirus is mainly assembled by the major capsid protein hexon. Folding and assembly of hexon require the viral encoded chaperone 100K, of which the detailed structure and chaperoning mechanism remain unknown. Here, we report the cryoEM structure of 100K in complex with a pre-mature hexon trimer. The structure shows that 100K dimers bind to the bottom double jelly-roll domains of the pre-mature hexon, mainly through a hook-like domain and a loop extruded from the dimerization domain. Additionally, a groove formed at the dimerization interface of 100K accommodates the N-terminal fragment 49-53 of an adjacent hexon protomer. Mutagenesis studies indicate that the interactions at the jelly-roll domain and the N-terminus of hexon are all essential for the proper folding and assembly of hexon. 100K binds and stabilizes the partially folded hexon, preventing premature aggregation of hexon, promoting the folding of the hexon top insertion loops, and facilitating hexon trimerization. Molecular mechanisms of the viral encoded chaperone 100K in capsid folding and assembly of adenovirus.,Li H, Shao L, Liu Z, Liu Q, Xiang Y Nat Commun. 2025 Apr 29;16(1):4013. doi: 10.1038/s41467-025-59301-4. PMID:40301360 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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