The FF ATP synthase in Synechocystis sp. PCC 6803 consists of two main sectors:
F: Catalyzes ATP synthesis/hydrolysis via αβγ subunits.
F: A membrane-embedded proton channel composed of subunits a (AtpB), b, and c .
Subunit a (AtpB) is essential for coupling proton movement with rotational mechanics in the F sector. Mutagenesis studies in Synechocystis have shown that modifications to other subunits (e.g., γ or ϵ) indirectly affect proton translocation efficiency and ATP synthesis rates, highlighting the interdependence of F and F components .
| Property | Description | Source |
|---|---|---|
| Host System | E. coli | |
| Tag | N-terminal His tag | |
| Amino Acid Range | 1–239 aa | |
| Molecular Function | Proton channel formation, rotational coupling with F sector |
Proton Translocation: AtpB works with subunit c to create a proton gradient-driven rotation, enabling ATP synthesis .
Regulatory Role: Interactions with γ and ϵ subunits modulate ATPase activity to prevent energy waste during dark conditions .
Deletion of regulatory regions in γ (e.g., β-hairpin) reduces ATP synthesis efficiency by ~30% in Synechocystis .
Truncation of the ϵ subunit’s C-terminal domain increases ATP hydrolysis activity, lowering intracellular ATP levels during prolonged darkness .
| Strain/Mutation | ATP Synthesis Rate | ATP Hydrolysis Activity | Survival in Darkness |
|---|---|---|---|
| Wild-Type Synechocystis | 100% | Baseline | High |
| γ Δ198–222 | ~70% | Elevated | Reduced |
| ϵ ΔC | ~85% | 2× baseline | Moderately Reduced |
These findings underscore AtpB’s role in maintaining energy homeostasis, particularly under stress conditions like nutrient limitation or darkness .
KEGG: syn:sll1322
STRING: 1148.SYNGTS_0164