2ze7 | pdb_00002ze7

Crystal Structure of adenosine phosphate-isopentenyltransferase complexed with zinc ion and substrate analog, DMASPP

spinqualitylabelsall models 2ze7, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ze7 is a 1 chain structure with sequence from "achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AMP, DST, ZN Related: 2ze5, 2ze6, 2ze8 Gene: tzs ("Achromobacter radiobacter" (Beijerinck and van Delden 1902) Bergey et al. 1934) Activity: Adenylate dimethylallyltransferase (AMP-dependent), with EC number 2.5.1.27 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IPTZ_AGRT5] Transfers dimethylallyl groups to AMP as part of the biosynthesis of cytokinin phytohormones. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The phytohormone cytokinin regulates plant growth and development. This hormone is also synthesized by some phytopathogenic bacteria, such as Agrobacterium tumefaciens, and is as a key factor in the formation of plant tumors. The rate-limiting step of cytokinin biosynthesis is catalyzed by adenosine phosphate-isopentenyltransferase (IPT). Agrobacterium IPT has a unique substrate specificity that enables it to increase trans-zeatin production by recruiting a metabolic intermediate of the host plant's biosynthetic pathway. Here, we show the crystal structures of Tzs, an IPT from A. tumefaciens, complexed with AMP and a prenyl-donor analogue, dimethylallyl S-thiodiphosphate. The structures reveal that the carbon-nitrogen-based prenylation proceeds by the SN2-reaction mechanism. Site-directed mutagenesis was used to determine the amino acid residues, Asp-173 and His-214, which are responsible for differences in prenyl-donor substrate specificity between plant and bacterial IPTs. IPT and the p loop-containing nucleoside triphosphate hydrolases likely evolved from a common ancestral protein. Despite structural similarities, IPT has evolved a distinct role in which the p loop transfers a prenyl moiety in cytokinin biosynthesis. Structural insight into the reaction mechanism and evolution of cytokinin biosynthesis.,Sugawara H, Ueda N, Kojima M, Makita N, Yamaya T, Sakakibara H Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2734-9. Epub 2008 Feb 7. PMID:18258747 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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