title: Structural characterization of the ribonuclease H-like type ASKHA superfamily kinase MK0840 from Methanopyrus kandleri.
abstract: Murein recycling is a process in which microorganisms recover peptidoglycan-degradation products in order to utilize them in cell wall biosynthesis or basic metabolic pathways. Methanogens such as Methanopyrus kandleri contain pseudomurein, which differs from bacterial murein in its composition and branching. Here, four crystal structures of the putative sugar kinase MK0840 from M. kandleri in apo and nucleotide-bound states are reported. MK0840 shows high similarity to bacterial anhydro-N-acetylmuramic acid kinase, which is involved in murein recycling. The structure shares a common fold with panthothenate kinase and the 2-hydroxyglutaryl-CoA dehydratase component A, both of which are members of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases. Local conformational changes in the nucleotide-binding site between the apo and holo forms are observed upon nucleotide binding. Further insight is given into domain movements and putative active-site residues are identified.
authors: Institute of Biochemistry, University of Cologne, Otto-Fischer-Strasse 12-14, 50674 Cologne, Germany.
authors: Magdalena
authors: M
authors: Schacherl
authors: Sandro
authors: S
authors: Waltersperger
authors: Ulrich
authors: U
authors: Baumann
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D019605:Euryarchaeota / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D007477:Ions / Q000378:metabolism; D008958:Models, Molecular; D009711:Nucleotides / Q000378:metabolism; D010770:Phosphotransferases / Q000737:chemistry* / Q000378:metabolism; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D016914:Ribonuclease H / Q000737:chemistry* / Q000378:metabolism
chemical_list: D007477:Ions; D009711:Nucleotides; D010770:Phosphotransferases; D016914:Ribonuclease H
keywords: ASKHA superfamily; domain closure; pseudomurein; sugar kinases