|Entry||Database: EMDB / ID: EMD-5136|
|Title||CryoEM Structure of Tubular Assembly of HIV-1 CA and Evidence for a Novel Interface|
|Sample||HIV-1 CA A92E:|
HIV-1 CA protein
|Biological species||Human immunodeficiency virus (Human immunodeficiency virus)|
|Method||helical reconstruction / cryo EM / Resolution: 16 Å|
|Authors||Byeon IL / Meng X / Jung J / Zhao G / Ahn J / Concel J / Aiken C / Gronenborn AM / Zhang P|
|Citation||Journal: Cell / Year: 2009|
Title: Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function.
Authors: In-Ja L Byeon / Xin Meng / Jinwon Jung / Gongpu Zhao / Ruifeng Yang / Jinwoo Ahn / Jiong Shi / Jason Concel / Christopher Aiken / Peijun Zhang / Angela M Gronenborn /
Abstract: Mature HIV-1 particles contain conical-shaped capsids that enclose the viral RNA genome and perform essential functions in the virus life cycle. Previous structural analysis of two- and ...Mature HIV-1 particles contain conical-shaped capsids that enclose the viral RNA genome and perform essential functions in the virus life cycle. Previous structural analysis of two- and three-dimensional arrays of the capsid protein (CA) hexamer revealed three interfaces. Here, we present a cryoEM study of a tubular assembly of CA and a high-resolution NMR structure of the CA C-terminal domain (CTD) dimer. In the solution dimer structure, the monomers exhibit different relative orientations compared to previous X-ray structures. The solution structure fits well into the EM density map, suggesting that the dimer interface is retained in the assembled CA. We also identified a CTD-CTD interface at the local three-fold axis in the cryoEM map and confirmed its functional importance by mutagenesis. In the tubular assembly, CA intermolecular interfaces vary slightly, accommodating the asymmetry present in tubes. This provides the necessary plasticity to allow for controlled virus capsid dis/assembly.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_5136.map.gz / Format: CCP4 / Size: 25.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
generated in cubic-lattice coordinate
|Voxel size||X=Y=Z: 2.15 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire HIV-1 CA A92E
|Entire||Name: HIV-1 CA A92E / Details: component name, HIV-1 CA protein / Number of components: 6|
-Component #1: protein, HIV-1 CA protein
|Protein||Name: HIV-1 CA protein / a.k.a: hexamerOligomer / Recombinant expression: Yes|
|Source||Species: Human immunodeficiency virus (Human immunodeficiency virus)|
|Specimen||Specimen state: Filament / Method: cryo EM|
|Helical parameters||Hand: RIGHT HANDED|
|Vitrification||Cryogen name: NITROGEN|
-Electron microscopy imaging
Model: Tecnai Polara / Image courtesy: FEI Company
|Imaging||Microscope: FEI POLARA 300|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: SPOT SCAN|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Holder: liquid nitrogen-cooled cryo specimen holder / Model: GATAN LIQUID NITROGEN|
|Processing||Method: helical reconstruction|
|3D reconstruction||Resolution: 16 Å / Resolution method: FSC 0.5|
-Atomic model buiding
|Modeling #1||Software: Chimera / Refinement space: REAL|
Input PDB model: 3DIK
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