Structure of aspartate β‐semialdehyde dehydrogenase from Francisella tularensis. Issue 1 (26th January 2018)

• Record Type: Journal Article
• Authors: Mank, N. J.; Pote, S.; Majorek, K.A.; Arnette, A. K.; Klapper, V. G.; Hurlburt, B. K.; Chruszcz, M.
• Is Part Of: Acta crystallographica. Volume 74:Issue 1(2018:Jan.)
• Page Start: 14
• Page End: 22
• Publication Date: 2018-01-26
• Subjects: amino‐acid biosynthesis -- lysine biosynthesis -- aspartate β‐semialdehyde dehydrogenase -- oxidoreductases -- Francisella tularensis -- tularemia; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X17017241
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of aspartate β‐semialdehyde dehydrogenase from F. tularensis has been determined. 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 + .