Researchers from the Seattle Structural Genomics Center for Infectious Diseases (SSGCID) have determined the three-dimensional protein structure of Mycobacterium avium phosphoserine phosphatase (SerB). The pathogen M. avium is a hardy, aerobic, Gram-positive bacterium that causes three different illnesses in humans - glandular fever in children, pneumonia in patients prone to lung disease, and generalized infection in AIDS patients.
Phosphoserine phosphatate plays a vital role in amino acid metabolism in all organisms. SerB catalyzes the reaction of 3-phosphoserine to L-serine, the final step in the biosynthesis of serine in both animals and bacteria.
The three-dimensional protein structure of Mycobacterium avium SerB is shown in green. Shown in grey is the superposed structure of SerB from M. jannaschii (1L7N).
For the first time researchers observed two new βαββαβ domains not observed in any other SerB crystal structures, requiring de novo phasing.
As a validated drug target, this protein's structure may provide a blueprint for structure-guided drug design.
For more information, please see the Protein Data Bank entry 3p96.
This work is to be published in the March issue of the Journal of Structural and Functional Genomics.
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Last Updated March 01, 2011
Last Reviewed March 01, 2011