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Research Abstracts Online
January - December 2011

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University of Minnesota Twin Cities
College of Biological Sciences
Medical School
Department of Biochemistry, Molecular Biology, and Biophysics

PI: Douglas H. Ohlendorf, Fellow

Structural Analysis of Macromolecules

The goal of these studies is to understand the structural basis of how macromolecules function. The current focus is on two groups of proteins: dixoygenases that use metal ions to cleave aromatic rings and proteins from gram-positive pathogens. Examples of dioxygenases are protocatechuate 3,4-dioxygenase (PCD), homoprotocatechuate 2,3-dioxygenase (HPCD), and 1,2-catechol dioxygenase (CTD). Examples of proteins from gram-positive pathogens are pyrogenic toxin superantigens (PTSAgs), exfoliative toxins (ETs), streptococcal C5a protease (SCPB), beta-toxin from S. aureus, and aggregation substance and the pheromone response protein PrgX from Enterococcus faecalis.

The researchers use resources at MSI to refine structures of substrate and inhibitor complexes of mutants of PCD, HPCD, and CTD, and to solve and refine the structures of several proteins from pathogens.

Group Members

Cathleen A. Earhart, Research Associate
Ed Hoeffner, Staff
Rebecca Hoeft, Graduate Student
Medora Huseby, Graduate Student
Ke Shi, Research Associate