Structure
All ABC transport proteins share a structural organization consisting of four core domains. These domains consist of two trans-membrane (T) domains and two cytosolic (A) domains. The T two domains alternate between an inward and outward facing orientation, and the alternation is powered by the hydrolysis of adenine triphosphate or ATP. ATP binds to the A subunits and it is then hydrolyzed to power the alternation, but the exact process by which this happens is not known. The four domains can be present in four separate polypeptides, which occur mostly in bacteria, or present in one or two multi-domain polypeptides. When the polypeptides are one domain, they are can be referred to as a full domain, and when they are two multi-domains they can be referred to as a half domain. The T domains are each built of typically 10 membrane spanning alpha helices, through which the transported substance can cross through the plasma membrane. Also, the structure of the T domains determines the specificity of each ABC protein. In the inward facing conformation, the binding site on the A domain is open directly to the surrounding aqueous solutions. This allows hydrophilic molecules to enter the binding site directly from the inner leaflet of the phospholipid bilayer. In addition, a gap in the protein is accessible directly from the hydrophobic core of the inner leaflet of the membrane bilayer. This allows hydrophobic molecules to enter the binding site directly from the inner leaflet of the phospholipid bilayer. After the ATP powered move to the outward facing conformation, molecules are released from the binding site and allowed to escape into the exoplasmic leaflet or directly into the extracellular medium.
Read more about this topic: ATP-binding Cassette Family
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