Structural studies of Nudix hydrolyases from Bacillus anthracis, the bacteria the produces the deadly toxin antrax
EMSL Project ID
7793
Abstract
Because of the interest in an anthrax due to issue related to Homeland Security, there is a great deal of interest in learning more about the bacteria that produces it, B. anthracis. Like Deinococcus radiodurans, the genome of B. anthracis contains may genes that are postulated to be Nudix hydrolyases. Nudix proteins are found in all organisms and are identified by the consensus sequence GX5EX7REUXEEXGU (where U = I, L, or V and X = any amino acid) that forms part of the catalytic site for the hydrolysis of a NUcleoside DIphosphate linked to some other moiety, X. The prototypical member of this family is the Escherichia coli MutT protein that catalyzes hydrolysis of nucleotide triphosphates with a preference for 8-oxo-dGTP. The primary function of Nudix proteins are to sanitize the cell by reducing the level of potentially mutagenic and/or toxic compounds and the accumulation of biochemical intermediates. Many Nudix hydroylases are critical for cell survive, hence, knowing the structure of these hydroylases from B. anthracis will aid the search for compounds that can ?knock-out? these hydroylases and hence also ?knock-out? these bacteria.
Project Details
Project type
Capability Research
Start Date
2004-05-13
End Date
2004-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members