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University of Pittsburgh researchers crack code of 3-D structure in key metabolic protein
Date:3/10/2008

gents called peptergents that they developed in their lab to carefully separate GlpD from the cell membrane and keep it in an active form to ensure that their studies revealed a physiologically relevant enzyme structure. The team then used detergents to crystallize the enzyme and screened the protein crystals in Pitts new state-of-the-art X-ray crystallography facility, directed by Dr. Yeh.

Next, they applied beams of high intensity parallel X-rays to the protein crystals in order to collect the diffraction data necessary to determine the proteins atomic configuration. These experiments were performed using cyclic particle accelerators at the Argonne National Laboratory in Illinois and the Paul Scherrer Institute in Switzerland. Called synchrotrons, these accelerators are the size of a football field and produce X-ray beams millions of times more intense than those generated by conventional X-ray machines. Highly advanced computational techniques were then used to analyze the diffraction data and to uncover, through complex mathematical approaches, the atomic matter in the crystals responsible for the diffraction. Ultimately, the unique 3-D topology of GlpD was deciphered, atom by atom.

The main role of GlpD in the cell is to remove hydrogen from a form of glycerol called glycerol-3-phosphate (G3P) to generate dihydroxyacetone phosphate (DHAP), a biochemical compound vital to the process of metabolizing the sugar-alcohol. In the process, electrons are produced and shuttled to a molecule called ubiquinone that works to power cellular respiration. Based on the structural information acquired in their study, Dr. Yehs team proposed mechanisms by which the enzyme carries out this fundamental metabolic reaction.

Their data revealed that GlpD is a dimer, or a protein with two subunits, that is embedded into and interacts substantially with the lipids that make up the cell membrane. This interaction with the membrane is required to keep the enzyme
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Contact: Michele Baum
BaumMD@upmc.edu
412-647-3555
University of Pittsburgh Schools of the Health Sciences
Source:Eurekalert

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