4bgb

Nucleotide-bound closed form of a putative sugar kinase MK0840 from Methanopyrus kandleri

spinqualitylabelsall models 4bgb, resolution 1.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bgb is a 2 chain structure with sequence from Methanopyrus kandleri AV19. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.34Å Ligands: ADP, CA, GOL, K, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8TX37_METKA Publication Abstract from PubMed 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. Structural characterization of the ribonuclease H-like type ASKHA superfamily kinase MK0840 from Methanopyrus kandleri.,Schacherl M, Waltersperger S, Baumann U Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2440-50. doi:, 10.1107/S0907444913022683. Epub 2013 Nov 19. PMID:24311585 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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