F-type ATP synthase of 8 subunits common to other ATPases, and 9 subunits unique to the Chlorophyta. Near neighbor interactions of the membrane subunits have been measured (Sánchez-Vásquez et al. 2017). The spinich enzyme has been solved at 3.4 Å resolution by cryoEM (Hahn et al. 2018). The protein has 26 protein subunits, 17 of them membrane embedded. Its c-ring has 14 c subunits. Hahn et al. 2018 observed 3 chloroplast F1F0 conformations with the central rotor stalled in different positions, and ring rotation seemed to be divided into 3 unequal stteps. The stoichiometrically mismatched c-ring of F0s (composed of 8 to 17 c-subunits) and the 3-fold symmetric F1 head are flexibly coupled (Murphy et al. 2019). Based on cryo EM 2.7 Å resolution structures, 13 rotary states suggest a mechanism of the rotational movement, and the functions of novel subunits are proposed (Murphy et al. 2019).
|Protein Name:||CBM40331.1 mitochondrial F1F0 ATP synthase associated 14 kDa protein [Polytomella sp. Pringsheim 198.80]|
|Species:||Polytomella sp. Pringsheim 198.80  |
1: MKLLPESLQQ EAATAAVVAS WVLWHLDTQL LPTIMREHKL HACWAAAAKR YNEKLFKLNP
61: SYDRVLSLPA VSKNQVLENV FHTAPKAPVE HLEKMVSANS KVYDALNLQS KRVLIWQVKP