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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #348597
Research Project: Reducing Peanut and Tree Nut Allergy

Location: Food Processing and Sensory Quality Research

Title: Structure of aspartate semialdehyde dehydrogenase from Francisella tularensis

Author
item MANK, N.J. - University Of South Carolina
item POTE, SWANANDI - University Of South Carolina
item MAJOREK, K. - University Of Virginia
item ARNETTE, A.K. - University Of South Carolina
item KLAPPER, VINCENT - University Of South Carolina
item Hurlburt, Barry
item CHRUSZCZ, MAKS - University Of South Carolina

Submitted to: Acta Crystallographica Section F: Structural Biology Communications
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/1/2017
Publication Date: 1/15/2018
Citation: Mank, N., Pote, S., Majorek, K., Arnette, A., Klapper, V., Hurlburt, B.K., Chruszcz, M. 2018. Structure of aspartate semialdehyde dehydrogenase from Francisella tularensis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. F74:14-22. https://doi.org/10.1107/S2053230X17017241.
DOI: https://doi.org/10.1107/S2053230X17017241

Interpretive Summary: Francisella tularensis is the causative agent of tularemia. Tularemia is a highly contagious disease that has a 30% mortality rate. Aspartate -semialdehyde dehydrogenase is an essential enzyme for amino acid biosynthesis and a potential target for novel antibiotics in this report, the 3-dimensional structure is solved by x-ray crystallography.

Technical Abstract: Aspartate -semialdehyde dehydrogenase (ASADH) is an enzyme involved in the diaminopimelate pathway of lysine biosynthesis. It is essential for the viability of many pathogenic bacteria and therefore has been the subject of considerable research for the generation of novel antibiotic compounds. This manuscript describes the first structure of ASADH from Francisella tularensis, the causative agent of tularemia and a potential bioterrorism agent. The structure was determined at 2.45 A ° resolution and has a similar biological assembly to other bacterial homologs. ASADH is known to be dimeric in bacteria and have extensive interchain contacts, which are thought to create a half-sites reactivity enzyme. ASADH from higher organisms shows a tetrameric oligomerization, which also has implications for both reactivity and regulation. This work analyzes the apo form of F. tularensis ASADH, as well as the binding of the enzyme to its cofactor NADP+.