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.
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Accession Number: | P74898 |
Protein Name: | VAPC-THERM |
Length: | 120 |
Molecular Weight: | 13142.00 |
Species: | Thermus thermophilus [274] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: |
Cell inner membrane1 / Peripheral membrane protein2 |
Substrate |
hydron |
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[1] “V-type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon.” Yokoyama K. et.al. 10788522
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1: MTGGLVLNAI SRAGGAMGGL GLIKSLAEKE KQLLERLEAA KKEAEERVKR AEAEAKALLE
61: EAEAKAKALE AQYRERERAE TEALLARYRE RAEAEAKAVR EKAMARLDEA VALVLKEVLP