4go7

The regulatory subunit of aspartate kinase in complex with threonine from Mycobacterium tuberculosis

spinqualitylabelsall models 4go7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4go7 is a 1 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: THR Related: 4go5 Gene: ask, Rv3709c, MT3812, MTV025.057c ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Activity: Aspartate kinase, with EC number 2.7.2.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AK_MYCTU] Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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