5A10

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

Summary for 5A10

• Entry DOI: 10.2210/pdb5a10/pdb
• Related: 5A11
• Descriptor: THIOCYANATE FORMING PROTEIN, ACETATE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: immune system, specifier protein, kelch protein, thlaspi arvense, field- penny cress, fe(ii) dependent
• Biological source: THLASPI ARVENSE
• Total number of polymer chains: 1
• Total formula weight: 39832.40

Authors

Krausze, J.,Gumz, F.,Wittstock, U. (deposition date: 2015-04-27, release date: 2015-08-26, Last modification date: 2024-01-10)

Primary citation

Gumz, F.,Krausze, J.,Eisenschmidt, D.,Backenkohler, A.,Barleben, L.,Brandt, W.,Wittstock, U.
The Crystal Structure of the Thiocyanate-Forming Protein from Thlaspi Arvense, a Kelch Protein Involved in Glucosinolate Breakdown.
Plant Mol.Biol., 89:67-, 2015

PubMed Abstract: 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 Å. TaTFP crystallized as homodimer. Each monomer forms a six-blade β-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 Fe(2+) 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.

PubMed: 26260516
DOI: 10.1007/S11103-015-0351-9

Experimental method

X-RAY DIFFRACTION (1.423 Å)