Molecular architecture and action of a proton pump

Proton pumps in the membrane surrounding plant and yeast cells maintain the intracellular pH. The resulting membrane potential drives the uptake of other ions and nutrients. Hence, the proper function of the proton pump is essential for survival of these organisms. Khlbrandt and colleagues at the Max Planck Institute of Biophysics in Frankfurt, Germany have generated a model of this key membrane protein and have deduced the mechanism by which it is regulated, as just published in Science.

The yeast proton pump is a member of the family of the so-called P-type ATPases. They are large membrane proteins which use the energy harnessed in adenosine triphosphate (ATP) to transport cations against a concentration gradient in an out of the cell. Other prominent family members include the sodium-potassium ATPase which regulates the heartbeat, the proton-potassium ATPase which acidifies the stomach, and the calcium ATPase which controls muscle contraction.

Detailed knowledge of the three-dimensional structure of any protein is the most important prerequisite for understanding how it works. The first, and so far only detailed structure of a P-type ion pump was that of the calcium ATPase from rabbit muscle, determined two years ago at Tokyo University by means x-ray crystallography. A less detailed structural model of the yeast proton ATPase was determined in 1998 by the group at the Max Planck Institute of Biophysics using the method of electron cryo-microscopy on two-dimensional crystals. Taking advantage of the molecular family resemblance, the Frankfurt group used the calcium pump structure to calculate a homology model of the proton pump. The model was fitted to the lower-resolution map determined by electron crystallography (fig.1). This revealed that the P-type ion pumps are surprisingly dynamic. The part which binds ATP rotates by more than 70 during the ion pumping cycle, enabling the release of energy which is then transmitted via conserved structural

Contact: Prof. W. Khlbrandt

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