Recombinant Citrobacter koseri ATP synthase subunit beta (atpD)
Description
ATP Synthase in Citrobacter koseri
ATP synthase is a critical enzyme complex for bacterial energy production, catalyzing ATP synthesis via a proton gradient. In C. koseri, ATP synthase comprises multiple subunits (e.g., α, β, γ, δ, ε, a, b, c), with subunit beta (atpD) forming part of the F1 catalytic core responsible for ATP synthesis .
Recombinant ATP Synthase Subunits
Research on recombinant C. koseri ATP synthase subunits highlights their structural and functional roles:
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Subunit c (atpE): Expressed in E. coli with a His-tag, this full-length protein (1-79 aa) forms the F0 proton channel. It is purified to >90% purity and stored as a lyophilized powder .
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Subunit delta (atpH): Recombinant atpH (1-177 aa) is expressed in E. coli with a predicted molecular weight of ~20 kDa. Its stability requires storage at -20°C/-80°C and reconstitution in glycerol-containing buffers .
Though subunit beta (atpD) is not directly described in the provided sources, its role in ATP synthesis is conserved across bacteria. For example, in E. coli, subunit beta binds ADP/ATP and undergoes conformational changes during catalysis .
Drug Development
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ATP Synthase Inhibitors: Computational studies identified four potential inhibitors (PubChem-25230613, PubChem-74936833, CHEMBL263035, PubChem-44208924) targeting C. koseri ATP synthase, with binding affinities up to -10.021 kcal/mol . These inhibitors disrupt energy metabolism, offering novel antibiotic strategies.
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Vaccine Design: Subtractive proteomics identified ATP synthase-associated proteins (e.g., DP-3-O-acyl-N-acetylglucosamine deacetylase) as vaccine candidates against C. koseri .
Immunological Roles
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C. koseri ATP production stimulates dendritic cells to induce IL-33, exacerbating allergic responses. This mechanism involves extracellular ATP binding to P2X7 receptors .
Antibiotic Resistance and Susceptibility
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Resistance Trends: C. koseri exhibits high susceptibility to carbapenems (89–92%), aminoglycosides (96–98%), and β-lactam/β-lactamase inhibitor combinations (84–94%) .
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Genetic Adaptations: Beta-lactamase genes (e.g., cdiA, cko) vary significantly between Citrobacter species, complicating treatment .
Future Directions
Product Specs
Target Background
KEGG: cko:CKO_00070
STRING: 290338.CKO_00070
