3.A.2.2.1 H+-translocating V-type ATPase. The 3-D structure is known (Lau and Rubinstein, 2012). More recently, Zhou and Sazanov 2019 solved cryo-EM structures of the intact Thermus thermophilus V/A-ATPase in three rotational
states with two substates. These structures indicate substantial
flexibility between V1 and Vo in a working enzyme,
which results from mechanical competition between central shaft
rotation and resistance from the peripheral stalks.
|
Accession Number: | Q72J68 |
Protein Name: | V-type sodium ATP synthase subunit K Homolog |
Length: | 99 |
Molecular Weight: | 9836.00 |
Species: | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [262724] |
Number of TMSs: | 3 |
Substrate |
hydron |
---|
1: MKKLLVTVLL AVFGALAFAA EEAAASGGLD RGLIAVGMGL AVGLAALGTG VAQARIGAAG
61: VGAIAEDRSN FGTALIFLLL PETLVIFGLL IAFILNGRL