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Tuberculosis
New findings from Washington University, Medical Department describe advances in tuberculosis
October 21st, 2008
"The crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase has been solved with bound effector, L-serine, and substrate, hydroxypyruvic acid phosphate, at resolutions of 2.7 and 2.4 angstrom, respectively. The subunits display the same extreme asymmetry as seen in the apostructure and provide insight into the mode of serine binding and closure of the active site," investigators in the United States report. "Mutagenesis studies confirm the identity of the main residues involved in serine binding and suggest that the poly glycine stretch in the loop that contains the locus for the 160 degrees rotation that leads to subunit asymmetry may have a...
Source: TB & Outbreaks Week (2008-10-21)
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