Recombinant Mycobacterium gilvum ATP synthase subunit alpha (atpA), partial

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Description

Definition and Basic Characteristics

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 .

Key Attributes:

AttributeDetails
Source OrganismMycobacterium gilvum (strain PYR-GCK)
Protein IDUniprot A4T8K0
Sequence CoveragePartial 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

Role in ATP Synthase Function

In mycobacteria, the α subunit:

  1. Binds nucleotides: Facilitates ATP synthesis via cooperative binding with β subunits .

  2. Regulates rotation: The C-terminal α extension (if present) inhibits ATP hydrolysis by interacting with γ subunits, preventing reverse proton pumping .

  3. Stabilizes the F₁ complex: Maintains structural integrity of the α₃β₃ hexamer .

Limitations in Available Data

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.

Hypothetical Applications

Based on homology to M. tuberculosis α subunits, potential uses include:

ApplicationRationale
Drug discoveryScreening for inhibitors targeting the α-γ interaction motif .
Biochemical assaysStudying nucleotide binding kinetics or subunit assembly in vitro.
Structural biologyMapping conserved/residue-specific interactions in mycobacterial ATP synthases .

Comparative Analysis of Mycobacterial α Subunits

SpeciesKey FeaturesRelevance to M. gilvum
M. tuberculosisC-terminal α extension (residues 514–549) inhibits ATP hydrolysis .Potential regulatory motif in M. gilvum.
M. smegmatisC-terminal α interacts with γ, stabilizing the "locked" state .Structural parallels in peripheral stalk assembly.
M. paratuberculosisPartial bδ subunit interactions critical for F₁-F₀ coupling .Shared peripheral stalk architecture.

Product Specs

Form
Lyophilized powder. We will ship the format we have in stock. If you have special format requirements, please note them when ordering.
Lead Time
Delivery time varies by purchase method and location. Consult your local distributor for specific delivery times. All proteins are shipped with blue ice packs by default. For dry ice shipment, contact us in advance; extra fees apply.
Notes
Avoid repeated freezing and thawing. Store working aliquots at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening. Reconstitute protein in sterile deionized water to 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer ingredients, storage temperature, and protein stability. Liquid form: 6 months at -20°C/-80°C. Lyophilized form: 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing. If you have a specific tag type requirement, please inform us.
Synonyms
atpA; Mflv_2316ATP synthase subunit alpha; EC 7.1.2.2; ATP synthase F1 sector subunit alpha; F-ATPase subunit alpha
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Protein Length
Partial
Purity
>85% (SDS-PAGE)
Species
Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK))
Target Names
atpA
Uniprot No.

Target Background

Function
Generates ATP from ADP using a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Database Links
Protein Families
ATPase alpha/beta chains family
Subcellular Location
Cell membrane; Peripheral membrane protein.

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