5a10

The crystal structure of Ta-TFP, a thiocyanate-forming protein involved in glucosinolate breakdown (space group C2)

spinqualitylabelsall models 5a10, resolution 1.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a10 is a 1 chain structure with sequence from Field penny-cress. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, NA Related: 5a11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Kelch repeat-containing proteins are involved in diverse cellular processes, but only a small subset of plant kelch proteins has been functionally characterized. Thiocyanate-forming protein (TFP) from field-penny cress, Thlaspi arvense (Brassicaceae), is a representative of specifier proteins, a group of kelch proteins involved in plant specialized metabolism. As components of the glucosinolate-myrosinase system of the Brassicaceae, specifier proteins determine the profile of bioactive products formed when plant tissue is disrupted and glucosinolates are hydrolyzed by myrosinases. Here, we describe the crystal structure of TaTFP at a resolution of 1.4 A. TaTFP crystallized as homodimer. Each monomer forms a six-blade beta-propeller with a wide "top" and a narrower "bottom" opening with distinct strand-connecting loops protruding far beyond the lower propeller surface. Molecular modeling and mutational analysis identified residues for glucosinolate aglucone and Fe2+ cofactor binding within these loops. As the first experimentally determined structure of a plant kelch protein, the crystal structure of TaTFP not only enables more detailed mechanistic studies on glucosinolate breakdown product formation, but also provides a new basis for research on the diverse roles and mechanisms of other kelch proteins in plants. The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown.,Gumz F, Krausze J, Eisenschmidt D, Backenkohler A, Barleben L, Brandt W, Wittstock U Plant Mol Biol. 2015 Aug 11. PMID:26260516 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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