8t1x

T4 highly immunogenic outer capsid protein C-terminal domain bound to the vertex-proximal gp23* capsomer of the isometric head in two preferred orientations

spinqualitylabelsall models 8t1x, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8t1x is a 8 chain structure with sequence from Escherichia phage T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CAPSH_BPT4 Major capsid protein that self-associates to form 160 hexamers, building most of the T=13 laevo capsid in association with 11 pentons made of gp24 and one dodecamer of gp20. Folding of gp23 requires the assistance of two chaperones, the host chaperone groL acting with the phage encoded gp23-specific chaperone, gp31. The capsid also contains two nonessential outer capsid proteins, Hoc and Soc, which decorate the capsid surface. Through binding to adjacent gp23 subunits, Soc reinforces the capsid structure.

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