5MCY
The structure of the mature HIV-1 CA pentamer in intact virus particles
Summary for 5MCY
| Entry DOI | 10.2210/pdb5mcy/pdb |
| EMDB information | 3466 |
| Descriptor | Capsid protein p24 (1 entity in total) |
| Functional Keywords | retrovirus, hiv-1, capsid, pentamer, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 20 |
| Total formula weight | 493085.36 |
| 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 Cited by 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: 27980210DOI: 10.1126/science.aah4972 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.8 Å) |
Structure validation
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