6PPI

Kaposi's sarcoma-associated herpesvirus (KSHV), C12 portal dodecamer structure

Summary for 6PPI

• Entry DOI: 10.2210/pdb6ppi/pdb
• Related: 6PPB 6PPD 6PPH
• EMDB information: 20430 20431 20432 20433 20436 20437
• Descriptor: Portal protein (1 entity in total)
• Functional Keywords: portal, capsid, genome, genome packaging, virus
• Biological source: Human herpesvirus 8 (HHV-8)
• Total number of polymer chains: 12
• Total formula weight: 817050.19

Authors

Gong, D.,Dai, X.,Jih, J.,Liu, Y.T.,Bi, G.Q.,Sun, R.,Zhou, Z.H. (deposition date: 2019-07-07, release date: 2019-09-11, Last modification date: 2024-03-20)

Primary citation

Gong, 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

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

Experimental method

ELECTRON MICROSCOPY (4.7 Å)