Extended Data Fig. 8: Superposition of structural domains of mBcs1.
From: Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein
a, Superposition of the AAA domain from apo (gray) and ATPγS-bound (magenta) structures. b, Superposition of the Bcs1-specific domain from apo (gray) and ATPγS-bound (magenta) structures. c, Interface between two neighboring AAA domains of mBcs1 undergoes a sliding movement upon ATP binding. The structure in the vicinity of ATP binding site for the apo structure (both subunit A and B) is shown as cartoon in gray. The Arg-finger residue R343 of subunit A of the apo mBcs1 is shown as a stick model. The subunit A of the ATPγS-bound mBcs1 is shown in cyan and its neighboring subunit B is shown in green. The residue R343 of subunit A of the ATPγS-bound structure is shown as a stick model. The two structures are superimposed based on subunit B. The distances from CA atoms of R343 of apo or ATPγS-bound Bcs1 to the γ-phosphate of ATP are given. d, Interface between two neighboring AAA domains of bacterial NtrC1 in ADP- or ADP•BeF3-bound forms. Distances from CA atoms of Arg-finger residue R299 to bound ADP•BeF3 are given. e, Interface between two neighboring AAA domains of mammalian AAA protein p97 D1 domain in ADP- or ATPγS-bound forms. Distances from CA atoms of Arg-finger residue R299 to γ-phosphate of ATPγS are given.
