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6PPB

Kaposi's sarcoma-associated herpesvirus (KSHV), C5 portal vertex structure

Summary for 6PPB
Entry DOI10.2210/pdb6ppb/pdb
EMDB information20430 20431 20432
DescriptorCapsid vertex component 1, Capsid vertex component 2, Large tegument protein deneddylase, ... (7 entities in total)
Functional Keywordsgenome, portal, capsid, genome packaging, virus, viral protein
Biological sourceHuman herpesvirus 8 (HHV-8)
More
Total number of polymer chains19
Total formula weight1651176.63
Authors
Gong, D.,Dai, X.,Jih, J.,Liu, Y.T.,Bi, G.Q.,Sun, R.,Zhou, Z.H. (deposition date: 2019-07-06, release date: 2019-09-11, Last modification date: 2024-11-06)
Primary citationGong, D.,Dai, X.,Jih, J.,Liu, Y.T.,Bi, G.Q.,Sun, R.,Zhou, Z.H.
DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV.
Cell, 178:1329-1343.e12, 2019
Cited by
PubMed Abstract: Assembly of Kaposi's sarcoma-associated herpesvirus (KSHV) begins at a bacteriophage-like portal complex that nucleates formation of an icosahedral capsid with capsid-associated tegument complexes (CATCs) and facilitates translocation of an ∼150-kb dsDNA genome, followed by acquisition of a pleomorphic tegument and envelope. Because of deviation from icosahedral symmetry, KSHV portal and tegument structures have largely been obscured in previous studies. Using symmetry-relaxed cryo-EM, we determined the in situ structure of the KSHV portal and its interactions with surrounding capsid proteins, CATCs, and the terminal end of KSHV's dsDNA genome. Our atomic models of the portal and capsid/CATC, together with visualization of CATCs' variable occupancy and alternate orientation of CATC-interacting vertex triplexes, suggest a mechanism whereby the portal orchestrates procapsid formation and asymmetric long-range determination of CATC attachment during DNA packaging prior to pleomorphic tegumentation/envelopment. Structure-based mutageneses confirm that a triplex deep binding groove for CATCs is a hotspot that holds promise for antiviral development.
PubMed: 31447177
DOI: 10.1016/j.cell.2019.07.035
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.3 Å)
Structure validation

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