5MD1

The structure of the mature HIV-1 CA hexameric lattice with curvature parameters: tilt=5, twist=0

Summary for 5MD1

• Entry DOI: 10.2210/pdb5md1/pdb
• EMDB information: 3469
• Descriptor: Capsid protein p24 (2 entities in total)
• Functional Keywords: retrovirus, hiv-1, capsid, lattice curvature, viral protein
• Biological source: Human immunodeficiency virus 1; More
• Total number of polymer chains: 14
• Total formula weight: 164774.68

Authors

Mattei, S.,Glass, B.,Hagen, W.J.H.,Kraeusslich, H.-G.,Briggs, J.A.G. (deposition date: 2016-11-10, release date: 2016-12-28, Last modification date: 2024-05-15)

Primary citation

Mattei, S.,Glass, B.,Hagen, W.J.,Krausslich, H.G.,Briggs, J.A.
The structure and flexibility of conical HIV-1 capsids determined within intact virions.
Science, 354:1434-1437, 2016

PubMed Abstract: HIV-1 contains a cone-shaped capsid encasing the viral genome. This capsid is thought to follow fullerene geometry-a curved hexameric lattice of the capsid protein, CA, closed by incorporating 12 CA pentamers. Current models for core structure are based on crystallography of hexameric and cross-linked pentameric CA, electron microscopy of tubular CA arrays, and simulations. Here, we report subnanometer-resolution cryo-electron tomography structures of hexameric and pentameric CA within intact HIV-1 particles. Whereas the hexamer structure is compatible with crystallography studies, the pentamer forms using different interfaces. Determining multiple structures revealed how CA flexes to form the variably curved core shell. We show that HIV-1 CA assembles both aberrant and perfect fullerene cones, supporting models in which conical cores assemble de novo after maturation.

PubMed: 27980210
DOI: 10.1126/science.aah4972

Experimental method

ELECTRON MICROSCOPY (8.2 Å)