Publication Abstract from PubMed
The aspartate kinase (AK) from Mycobacterium tuberculosis (Mtb) catalyzes the biosynthesis of aspartate family amino acids, including lysine, threonine, isoleucine and methionine. We determined the crystal structures of the regulatory subunit of aspartate kinase from Mtb alone (referred to as MtbAKbeta) and in complex with threonine (referred to as MtbAKbeta-Thr) at resolutions of 2.6 A and 2.0 A, respectively. MtbAKbeta is composed of two perpendicular non-equivalent ACT domains [aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)] per monomer. Each ACT domain contains two alpha helices and four antiparallel beta strands. The structure of MtbAKbeta shares high similarity with the regulatory subunit of the aspartate kinase from Corynebacterium glutamicum (referred to as CgAKbeta), suggesting similar regulatory mechanisms. Biochemical assays in our study showed that MtbAK is inhibited by threonine. Based on crystal structure analysis, we discuss the regulatory mechanism of MtbAK.
Structural view of the regulatory subunit of aspartate kinase from Mycobacterium tuberculosis.,Yang Q, Yu K, Yan L, Li Y, Chen C, Li X Protein Cell. 2011 Sep;2(9):745-54. Epub 2011 Oct 6. PMID:21976064[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
