University of Pittsburgh researchers crack code of 3-D structure in key metabol...(e to the interior of the cell. As a resu...),Health

Date:3/10/2008

e to the interior of the cell. As a result, it is technically challenging to produce enough highly purified and active protein to obtain clear, relevant information about the enzymes atomic structure. This study marks the highest resolution structure of a monotopic membrane protein that scientists have solved to date, and is one of only a handful of structures of this important class of membrane proteins that have been determined.

These findings and data help to fill an important scientific and technical gap in the structural field and present new information and ideas about how the enzyme works and the importance of the cell membrane in stabilizing the enzyme and in processes related to energy production, said Dr. Yeh, who published the paper along with postdoctoral research associate Unmesh N. Chinte, Ph.D., and research assistant professor, Shoucheng Du, Ph.D., both in Pitts Department of Structural Biology.

Studying the proteins and enzymes involved in oxidative and glycerol metabolism, as well as characterizing their structures, functions and regulatory relationships, has been a major research interest of Dr. Yehs lab. It took Dr. Yeh and her colleagues only three months an unusually short time to decipher the set of 3-D structures of GlpD isolated from E. coli bacteria, thanks to other methodologies they developed in earlier studies.

Rather than make conclusions based on a single structure, the team additionally determined the structures of GlpD bound with its metabolic product and several substrate analogues to evaluate the enzyme in its native and combined forms. By careful unraveling of this collection of structures, researchers could gain a more complete understanding of how the enzyme functions, details about how GlpD interacts with the membrane, works to catalyze the enzymatic reaction, and links to cellular-energy production.

As part of these challenging studies, the Pitt researchers used novel peptide-based deter
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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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