6SSK

Human endogenous retrovirus (HML2) mature capsid assembly, D5 capsule

Summary for 6SSK

• Entry DOI: 10.2210/pdb6ssk/pdb
• EMDB information: 10295 10296 10297 10298
• Descriptor: Endogenous retrovirus group K member 24 Gag polyprotein (1 entity in total)
• Functional Keywords: mature retrovirus capsid assembly, viral protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 9
• Total formula weight: 248134.39

Authors

Acton, O.J.H.,Taylor, I.A.,Rosenthal, P.B. (deposition date: 2019-09-08, release date: 2020-01-01, Last modification date: 2024-11-06)

Primary citation

Acton, O.,Grant, T.,Nicastro, G.,Ball, N.J.,Goldstone, D.C.,Robertson, L.E.,Sader, K.,Nans, A.,Ramos, A.,Stoye, J.P.,Taylor, I.A.,Rosenthal, P.B.
Structural basis for Fullerene geometry in a human endogenous retrovirus capsid.
Nat Commun, 10:5822-5822, 2019

PubMed Abstract: The HML2 (HERV-K) group constitutes the most recently acquired family of human endogenous retroviruses, with many proviruses less than one million years old. Many maintain intact open reading frames and provirus expression together with HML2 particle formation are observed in early stage human embryo development and are associated with pluripotency as well as inflammatory disease, cancers and HIV-1 infection. Here, we reconstruct the core structural protein (CA) of an HML2 retrovirus, assemble particles in vitro and employ single particle cryogenic electron microscopy (cryo-EM) to determine structures of four classes of CA Fullerene shell assemblies. These icosahedral and capsular assemblies reveal at high-resolution the molecular interactions that allow CA to form both pentamers and hexamers and show how invariant pentamers and structurally plastic hexamers associate to form the unique polyhedral structures found in retroviral cores.

PubMed: 31862888
DOI: 10.1038/s41467-019-13786-y

Experimental method

ELECTRON MICROSCOPY (3.18 Å)