Recombinant Aeromonas salmonicida ATP synthase subunit delta (atpH)
Description
Introduction
The ATP synthase subunit delta (atpH) from Aeromonas salmonicida is a critical component of the bacterial ATP synthase complex, which catalyzes the synthesis of ATP through proton translocation across the membrane. This subunit belongs to the F1 sector of the ATP synthase and plays a structural and regulatory role in the enzyme’s function. Recombinant production of atpH has gained attention for its potential applications in vaccine development and bacterial pathogenesis research .
Structure and Function
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Protein Sequence: The atpH subunit consists of 177 amino acids (UniProt ID: A4STP6) and features a sequence characterized by hydrophilic regions and motifs critical for subunit interactions. Its primary structure includes domains involved in binding to other ATP synthase subunits and stabilizing the F1 sector .
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Role in ATP Synthase: Subunit delta is part of the stator component of the ATP synthase, ensuring mechanical stability and facilitating proton-driven rotation of the rotor (c-ring and γ-subunit complex). It interacts directly with the α and β subunits of the F1 sector to regulate catalytic activity .
Host Systems
| Host Organism | Expression System | Protein Length | Purity |
|---|---|---|---|
| E. coli | Recombinant | Full-length | >85% |
| Yeast | Recombinant | Full-length | >85% |
| Baculovirus | Recombinant | Full-length | N/A |
| Mammalian Cell | Recombinant | Full-length | N/A |
Applications
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Vaccine Development: The atpH subunit is being explored as a candidate for vaccines targeting Aeromonas infections, leveraging its immunogenic properties to induce protective immunity .
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Pathogenesis Research: Studies focus on understanding ATP synthase’s role in bacterial survival, particularly under stress conditions, and its potential as a drug target .
Research Findings
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Subunit Interactions: Mutational studies reveal that atpH interacts with the γ-loop of the ATP synthase to modulate catalytic efficiency, a feature absent in human homologs .
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Antibacterial Targets: The unique structural motifs of atpH (e.g., hydrophobic regions) make it a candidate for species-specific inhibitors, reducing off-target effects .
Product Specs
Target Background
KEGG: asa:ASA_4353
STRING: 382245.ASA_4353
