Abc transporters

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ABC transporters 'are the largest family of membrane transporters'. ABC transporters are integral proteins, using energy from the hydrolysis of ATP to pump molecules across the memebrane. These transporters are used to transport small molecules across the cell membrane. Each ABC traporter contains two ATP-binding domains called cassettes. As ATP binds to the casettes they under go dimerization. Each cassette protrudes into cytosol. There are two halves of each transporter, of which they can either be made of a single peptide or by one or more polypeptides, which form a similiar structure. When ATP isn't present the binding site is expressed on either the intracellular or extracellular space. As the ATP binds it causes a conformational change in the ABC transporter, which exposes the substrate binding site on the opposite face. As a molecule of ATP is hydrolysed, this is followed by the dissociation of ADP. The ATP hydrolysis returns the transporter to its original form [1][2].

References

  1. P. M. Jones A. M. George . (2004). The ABC transporter structure and mechanism: perspectives on recent research. Cellular and Molecular Life Sciences CMLS . Volume 61, p682-699.
  2. B Alberts, A Johnson, J Lewis, Martin Raff, K Raff, K Roberts, P Walter, J Wilson, T Hunt (2008). Molecular Biology of The Cell 5th Edition. New York: Garland Science. p660-p665.
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