1. Structure of aspartate β-semialdehyde dehydrogenase from Francisella tularensis.
- Author
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Mank NJ, Pote S, Majorek KA, Arnette AK, Klapper VG, Hurlburt BK, and Chruszcz M
- Subjects
- Amino Acid Sequence, Aspartate-Semialdehyde Dehydrogenase genetics, Aspartate-Semialdehyde Dehydrogenase metabolism, Bacterial Proteins genetics, Bacterial Proteins metabolism, Catalytic Domain, Crystallography, X-Ray, Francisella tularensis genetics, Models, Molecular, NADP metabolism, Protein Structure, Quaternary, Recombinant Proteins chemistry, Sequence Homology, Amino Acid, Structural Homology, Protein, Aspartate-Semialdehyde Dehydrogenase chemistry, Bacterial Proteins chemistry, Francisella tularensis enzymology
- Abstract
Aspartate β-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 Å 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
+ .- Published
- 2018
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