8PUC
Structure of immature HTLV-1 CA-NTD from in vitro assembled MA126-CANC tubes: axis angle 05 degrees
Summary for 8PUC
| Entry DOI | 10.2210/pdb8puc/pdb |
| EMDB information | 17929 17930 17931 17932 17933 17934 17935 17936 17937 17938 17939 17940 17941 17942 17943 |
| Descriptor | Gag protein (Fragment) (1 entity in total) |
| Functional Keywords | retrovirus, htlv, immature capsid, ca, ca-ntd, viral protein |
| Biological source | Human T-cell leukemia virus type I |
| Total number of polymer chains | 3 |
| Total formula weight | 41909.43 |
| Authors | Obr, M.,Percipalle, M.,Chernikova, D.,Yang, H.,Thader, A.,Pinke, G.,Porley, D.,Mansky, L.M.,Dick, R.A.,Schur, F.K.M. (deposition date: 2023-07-17, release date: 2023-08-23, Last modification date: 2024-09-18) |
| Primary citation | Obr, M.,Percipalle, M.,Chernikova, D.,Yang, H.,Thader, A.,Pinke, G.,Porley, D.,Mansky, L.M.,Dick, R.A.,Schur, F.K.M. Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice. Nat.Struct.Mol.Biol., 2024 Cited by PubMed Abstract: Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron tomography studies of HTLV-1 virus-like particles assembled in vitro, as well as derived from cells. This work shows that HTLV-1 uses a distinct mechanism of Gag-Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature capsid (CA) tubular arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal domain of CA. Mutagenesis analysis supports this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the C-terminal domain of CA. These results provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain why HTLV-1 particles are morphologically distinct. PubMed: 39242978DOI: 10.1038/s41594-024-01390-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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