Fig. 3: Cryo-EM structure of full-length Bpa from M. tuberculosis. | Nature Communications

Fig. 3: Cryo-EM structure of full-length Bpa from M. tuberculosis.

From: Substrates bind to residues lining the ring of asymmetrically engaged bacterial proteasome activator Bpa

Fig. 3

A Top view of the cryo-EM map of full-length Bpa. B Side view of the full-length Bpa map. C Exemplary stretch of residues belonging to helix H3 and the H3-H4 linker of Bpa displaying confident modeling of residues into the density map. D Structure of the Bpa dodecameric ring. Each Bpa protomer is colored differently. E The crystal structure of Bpa (PDB 5LFJ, green) shows ordered C-terminal extensions of helix H4 to residue L148. The cryo-EM map of full-length Bpa (purple) is resolved up to residue Q140 indicating considerable flexibility beyond that point.

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