Fig. 4: Conformational change in the Bap31_vDED domain upon complex formation with Fis1_ΔTM. | Communications Biology

Fig. 4: Conformational change in the Bap31_vDED domain upon complex formation with Fis1_ΔTM.

From: Crystal structure of Fis1 and Bap31 provides information on protein-protein interactions at mitochondria-associated ER membranes

Fig. 4

A Overview of dimeric Bap31_vDED in a previous report and in the present study. Dimeric Bap31_vDED under acidic conditions (chains A and B, green, PDB code: 4JZP), dimeric Bap31_vDED under neutral conditions (chains A and D, yellow, PDB code: 4JZL), and two heterodimers of Bap31_vDED bound to Fis1_ΔTM (chains G−F and D−E, pink and orange, in this study) are shown. The terminal residues at the distal C-terminus of Bap31_vDED in the structural model are indicated in each chain. B Chain F of the complex structure superimposed on chain A of the previously reported Bap31_vDED structures, showing the displacement and movement of chain G relative to chain B and chain D.

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