4q0k

Crystal Structure of Phytohormone Binding Protein from Medicago truncatula in complex with gibberellic acid (GA3)

spinqualitylabelsall models 4q0k, resolution 1.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q0k is a 1 chain structure with sequence from Barrel medic. This structure supersedes the now removed PDB entry 3us7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GA3, GOL Related: 2flh, 4jhg, 2qim, 1xdf, 1ifv, 1icx, 4psb Gene: mtphbp, MTR_3g055120 (Barrel medic) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 approximately 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). Specific binding of gibberellic acid by Cytokinin-Specific Binding Proteins: a new aspect of plant hormone-binding proteins with the PR-10 fold.,Ruszkowski M, Sliwiak J, Ciesielska A, Barciszewski J, Sikorski M, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2014 Jul 1;70(Pt 7):2032-41. doi:, 10.1107/S1399004714010578. Epub 2014 Jun 29. PMID:25004979 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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