5tk7 | pdb_00005tk7

Structure of the HD-domain phosphohydrolase OxsA with Oxetanocin-A triphosphate bound

spinqualitylabelsall models 5tk7, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tk7 is a 1 chain structure with sequence from Priestia megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.904Å Ligands: 7D4, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O24769_PRIMG Publication Abstract from PubMed HD domain phosphohydrolase enzymes are characterized by a conserved set of histidine and aspartate residues that coordinate an active site metallocenter. Despite the important roles these enzymes play in nucleotide metabolism and signal transduction, few have been both biochemically and structurally characterized. Here, we present X-ray crystal structures and biochemical characterization of the Bacillus megaterium HD domain phosphohydrolase OxsA, involved in the biosynthesis of the antitumor, antiviral, and antibacterial compound oxetanocin-A. These studies reveal a previously uncharacterized reaction for this family; OxsA catalyzes the conversion of a triphosphorylated compound into a nucleoside, releasing one molecule of inorganic phosphate at a time. Remarkably, this functionality is a result of the OxsA active site, which based on structural and kinetic analyses has been tailored to bind the small, four-membered ring of oxetanocin-A over larger substrates. Furthermore, our OxsA structures show an active site that switches from a dinuclear to a mononuclear metal center as phosphates are eliminated from substrate. An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.,Bridwell-Rabb J, Kang G, Zhong A, Liu HW, Drennan CL Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13750-13755. Epub 2016 Nov 14. PMID:27849620 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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