Fig. 4: The occluded structure with bound ATP.
From: Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria
a The occluded structure with bound ATP, CtAtm1occl/ATP, with the supporting cryo-EM density for ATP (red) and the protein colored as in Fig. 1d. b Close-view of the occluded highly electropositive pocket. Residues Y232, E403, and V400 divide the pocket next to the inner gate. The interactions between H240, F396, and S399 separate the pocket from the pathway on the other side of F396. c Comparison of the conformation of transmembrane helix TM6 between the inward-open (CtAtm1inw-opn, gray), the inward-facing partially occluded (CtAtm1inw-opn-occl, green), the occluded (CtAtm1occl, brown), and AtAtm3 outward-facing (AtAtm3OF, cyan) states, demonstrating a considerable rearrangement of F396. d Identical view as in panel c of the equivalent states of the prokaryotic Atm1 member NaAtm1: inward-open (PDB-ID 6VQU, gray), inward-facing occluded (PDB-ID 4MRS, green), and occluded (PDB-ID 6PAO, brown). In addition, the closed post-hydrolysis state of NaAtm1 is shown (PDB-ID 6VQT, cyan).
