Fig. 1: Transport cycle, function, and inward-open structure.
From: Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria
a Atm1-type ABC proteins presumably exploit a transport mechanism that includes inward-facing, occluded, outward-facing, and closed conformations, and requires ATP and cargo to turnover. b CtAtm1-discs size-exclusion chromatography profile and associated Coomassie-stained SDS-PAGE analysis (nanodisc reconstitutions were performed more than three independent times). c ATPase activity of CtAtm1 in detergent solution and 20 µM GSH, GSSG, or cluster. Data points represent the means of three independent measurements and error bars indicate standard deviation. d Cryo-EM map of CtAtm1 in the inward-facing open conformation, CtAtm1inw-opn, with one monomer shown in blue and another in brown. e The structure of CtAtm1inw-opn with 12 transmembrane helices and two NBDs. f Structural comparison of CtAtm1inw-opn (blue and brown) with the equivalent conformation of NaAtm1 colored green (PDB-ID 6VQU, green) and AtAtm3 colored gray (PDB-ID 7N58, gray). g Surface charge of CtAtm1inw-opn as observed from the mitochondrial matrix. h Close-view of the positively charged cavity with residue pairs Asn395 and Phe396 (same orientation as in panel g).
