Recombinant Mycobacterium gilvum ATP synthase subunit alpha (atpA), partial refers to a truncated form of the ATP synthase α subunit protein derived from Mycobacterium gilvum, a non-tuberculous mycobacterium. This recombinant protein is engineered for laboratory use, typically expressed in heterologous systems (e.g., E. coli) and purified for biochemical studies. The term "partial" indicates that the protein lacks certain regions of the full-length α subunit, though specific truncation boundaries are not explicitly detailed in available sources .
| Attribute | Details |
|---|---|
| Source Organism | Mycobacterium gilvum (strain PYR-GCK) |
| Protein ID | Uniprot A4T8K0 |
| Sequence Coverage | Partial sequence: MAELIISASD... (N-terminal segment) to ...APASDAAGFKWLAP (C-terminal segment) |
| Purity | >85% (SDS-PAGE) |
| Storage | -20°C or -80°C; working aliquots at 4°C for up to 1 week |
In mycobacteria, the α subunit:
Binds nucleotides: Facilitates ATP synthesis via cooperative binding with β subunits .
Regulates rotation: The C-terminal α extension (if present) inhibits ATP hydrolysis by interacting with γ subunits, preventing reverse proton pumping .
Stabilizes the F₁ complex: Maintains structural integrity of the α₃β₃ hexamer .
Despite its availability as a research reagent, no peer-reviewed studies explicitly investigate the M. gilvum partial α subunit. Key gaps include:
Mechanistic studies: No data on its ATPase activity, PMF coupling, or γ-subunit interaction dynamics.
Structural insights: Cryo-EM or X-ray crystallography data for M. gilvum’s α subunit are absent.
Comparative analysis: Differences between M. gilvum’s α subunit and those of pathogenic mycobacteria (e.g., M. tuberculosis) remain unexplored.
Based on homology to M. tuberculosis α subunits, potential uses include:
KEGG: mgi:Mflv_2316
STRING: 350054.Mflv_2316