ATP5D Human
Description
ATP5D produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (23-168 a.a.) and having a molecular mass of 17.3kDa.
ATP5D is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
ATP Synthase Subunit D, also known as ATP5PD, is a crucial component of the mitochondrial ATP synthase complex, often referred to as Complex V. This enzyme complex plays a pivotal role in cellular energy production by synthesizing adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate, utilizing the proton gradient generated by the electron transport chain across the inner mitochondrial membrane .
The mitochondrial ATP synthase is a multi-subunit protein complex with an approximate molecular weight of 550 kDa . It consists of two main functional domains: F1, located in the mitochondrial matrix, and Fo, embedded in the inner mitochondrial membrane . ATP Synthase Subunit D is part of the peripheral stalk, which connects these two domains and plays a critical role in the structural stability and function of the enzyme .
The peripheral stalk, including Subunit D, prevents the rotation of the catalytic F1 domain relative to the Fo domain during ATP synthesis. This stabilization is essential for the proper functioning of the rotary nanomotor mechanism of ATP synthase, which is responsible for the phosphorylation of ADP to ATP .
The ATP5PD gene encodes the ATP Synthase Subunit D protein. Mutations in this gene can lead to various mitochondrial diseases, including Bardet-Biedl Syndrome 18 and other mitochondrial dysfunctions . The human recombinant form of this protein is often used in research to study its structure, function, and role in mitochondrial pathologies.
ATP synthase is the smallest known biological nanomotor and is crucial for ATP production, which is the primary energy currency in all living cells . The enzyme operates through a process known as oxidative phosphorylation, where the energy from the proton gradient is harnessed to drive the synthesis of ATP. This process is vital for maintaining the energy balance within cells and supporting various metabolic pathways .
Deficiencies or malfunctions in ATP synthase, including Subunit D, can lead to severe mitochondrial diseases. These conditions often manifest as neuromuscular disorders, metabolic syndromes, and other systemic issues due to impaired cellular energy production . Understanding the structure and function of ATP Synthase Subunit D is therefore critical for developing therapeutic strategies for these diseases.
