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

energetically and functionally stable so that it doesnt collapse on itself, the PNAS study reports.

Dr. Yehs team also found that the enzyme is made up of two major domains: a soluble extracellular cap and a FAD-binding region, whose base is rooted in the membrane. The location of the enzymes active site where the chemical reaction actually occurs is at this FAD-binding region. G3P fastens tightly here, much like a key fitting into a lock, and is then transformed into DHAP. The researchers also proposed a docking site for where ubiquinone binds to the enzyme to accept electrons produced in the reaction. Eventually, ubiquinone feeds these electrons into respiration to produce the crucial energy to fuel cellular processes.

In addition, Dr. Yehs team discovered a never-before-seen type of protein fold consisting of about 100 amino acids in the cap domain of GlpD. They also identified areas where other proteins might bind to regulate the enzymes activity and transmit chemical signals.

With the GlpD structure in hand, Dr. Yehs team is already examining how mutating, or changing, certain amino acids in the enzyme affects its function and fold. These studies target the roles that these specific amino acids play in enzymatic function and regulation of activity. These questions are important because glycerol metabolism is a key link between sugar and fatty acid metabolism. The Pitt group also has determined the atomic resolution structures of other enzymes involved in mediating glycerol and oxidative metabolism. In all, these structural results provide some of the first three-dimensional views of these highly important proteins and enzymes.


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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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