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6PPD

Kaposi's sarcoma-associated herpesvirus (KSHV), C1 penton vertex register, CATC-absent structure

Summary for 6PPD
Entry DOI10.2210/pdb6ppd/pdb
Related6PPB
EMDB information20430 20431 20432 20433
DescriptorSmall capsomere-interacting protein, Major capsid protein, Triplex capsid protein 1, ... (4 entities in total)
Functional Keywordscapsid, tegument, vertex, complex, virus, viral protein
Biological sourceHuman herpesvirus 8 (HHV-8)
More
Total number of polymer chains16
Total formula weight1070723.63
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 (3.7 Å)
Structure validation

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数据于2025-08-27公开中

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