4PSB
Crystal Structure of Phytohormone Binding Protein from Vigna radiata in complex with gibberellic acid (GA3)
Summary for 4PSB
| Entry DOI | 10.2210/pdb4psb/pdb |
| Related | 2flh 2qim 3us7 4jhg |
| Descriptor | Cytokinin-specific binding protein, GIBBERELLIN A3 (3 entities in total) |
| Functional Keywords | cytokinin specific binding protein (csbp), pr-10 fold, gibberellin, cytokinin, plant hormone binding, plant protein |
| Biological source | Vigna radiata (mung bean) |
| Total number of polymer chains | 1 |
| Total formula weight | 17959.23 |
| Authors | Ruszkowski, M.,Sikorski, M.,Jaskolski, M. (deposition date: 2014-03-07, release date: 2014-07-23, Last modification date: 2023-09-20) |
| Primary citation | Ruszkowski, M.,Sliwiak, J.,Ciesielska, A.,Barciszewski, J.,Sikorski, M.,Jaskolski, M. Specific binding of gibberellic acid by Cytokinin-Specific Binding Proteins: a new aspect of plant hormone-binding proteins with the PR-10 fold. Acta Crystallogr.,Sect.D, 70:2032-2041, 2014 Cited by PubMed Abstract: Pathogenesis-related proteins of class 10 (PR-10) are a family of plant proteins with the same fold characterized by a large hydrophobic cavity that allows them to bind various ligands, such as phytohormones. A subfamily with only ~20% sequence identity but with a conserved canonical PR-10 fold have previously been recognized as Cytokinin-Specific Binding Proteins (CSBPs), although structurally the binding mode of trans-zeatin (a cytokinin phytohormone) was found to be quite diversified. Here, it is shown that two CSBP orthologues from Medicago truncatula and Vigna radiata bind gibberellic acid (GA3), which is an entirely different phytohormone, in a conserved and highly specific manner. In both cases a single GA3 molecule is found in the internal cavity of the protein. The structural data derived from high-resolution crystal structures are corroborated by isothermal titration calorimetry (ITC), which reveals a much stronger interaction with GA3 than with trans-zeatin and pH dependence of the binding profile. As a conclusion, it is postulated that the CSBP subfamily of plant PR-10 proteins should be more properly linked with general phytohormone-binding properties and termed phytohormone-binding proteins (PhBP). PubMed: 25004979DOI: 10.1107/S1399004714010578 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.42 Å) |
Structure validation
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