Recombinant Agrobacterium tumefaciens ATP synthase subunit a (atpB)
Description
Structure and Function of ATP Synthase in A. tumefaciens
ATP synthase in A. tumefaciens comprises two sectors:
-
F1: Catalytic head (α3β3γδε subunits) for ATP synthesis.
-
Fo: Membrane-embedded proton channel (ab2c10 subunits).
The α-subunit (atpA) forms part of the F1 hexamer, binding nucleotides and facilitating conformational changes during ATP synthesis . Recombinant atpA is produced to study its role in enzyme assembly and catalysis .
Recombinant Production and Applications
Recombinant atpA is commercially available as a partial protein (MyBioSource.com) . Key features include:
| Parameter | Description |
|---|---|
| Source organism | Agrobacterium tumefaciens |
| Expressed system | Likely E. coli (common for recombinant proteins) |
| Applications | Enzyme kinetics, antibody production, structural studies |
| Purity | ≥90% (typical for commercial recombinant proteins) |
| Molecular weight | ~55 kDa (predicted for partial sequence) |
This tool enables studies on ATP synthase’s role in bacterial metabolism and pathogenicity, including A. tumefaciens’ T-DNA transfer system, which relies on VirB11 ATPase homologs .
Assembly Mechanisms and Chaperones
ATP synthase assembly requires chaperones like Atp11 and Atp12, which prevent misfolding of α- and β-subunits . Key findings:
In A. tumefaciens, homologs of these chaperones likely exist, given conserved ATP synthase structures across bacteria . For example:
-
VirB11 (a type IV secretion ATPase) self-assembles into homomultimers, requiring ATP binding for functional C-terminal interactions .
-
Dominant-negative VirB11 mutants disrupt T-DNA transfer by titrating native proteins .
Cross-Organism Insights
Studies in Arabidopsis and yeast reveal principles applicable to A. tumefaciens:
-
Knockdown effects: Depleting ATP synthase subunits (e.g., atp1 in Arabidopsis) reduces complex stability and ATP synthesis without affecting electron transport chain components .
-
PPR proteins: Custom RNA-binding proteins can selectively deplete mitochondrial atp1 mRNA, validating subunit-specific roles .
-
Operon organization: Chloroplast atp genes (e.g., atpB/E, atpI/H/F/A) require RNA-binding proteins (e.g., BFA2) for transcript stabilization and translation .
Research Gaps and Future Directions
-
Structural resolution: No high-resolution structures of A. tumefaciens ATP synthase exist. Cryo-EM studies could clarify atpA’s role.
-
Chaperone homology: Whether A. tumefaciens employs Atp11/Atp12-like chaperones remains unconfirmed .
-
Pathogenicity link: ATP synthase’s contribution to A. tumefaciens virulence is underexplored compared to VirB systems .
Key Citations
Product Specs
Note: We will prioritize shipping the format currently in stock. However, if you have specific requirements for the format, please specify them during order placement. We will prepare your order accordingly.
Note: All our proteins are shipped with standard blue ice packs. If you require dry ice shipping, please notify us in advance. Additional fees will apply.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Target Background
KEGG: atu:Atu0714
STRING: 176299.Atu0714
