Báo cáo khoa học: Cytokinin-induced structural adaptability of a Lupinus luteus PR-10 protein

Cytokinin-induced structural adaptability of a Lupinus luteus PR-10 protein

Authors: Humberto Fernandes, Anna Bujacz, Grzegorz Bujacz, Filip Jelen, Michal Jasinski, Piotr Kachlicki, Jacek Otlewski, Michal M. Sikorski, and Mariusz Jaskolski

Field: Biochemistry, Structural Biology, Plant Physiology

Document Summary: This study investigates the structural adaptability of the *Lupinus luteus* PR-10 protein (LIPR-10.2B) when interacting with N,N’-diphenylurea (N,N’-DPU), a synthetic cytokinin. Through crystallographic analysis at 1.95 Å resolution, the research reveals that four N,N’-DPU molecules bind within the protein’s hydrophobic cavity. The binding of these ligands induces conformational changes in the protein, particularly in the C-terminal α3-helix, leading to an increased cavity volume. This structural flexibility suggests that PR-10 proteins, including LIPR-10.2B, may function as reservoirs for cytokinin molecules within plant cells. The study also includes calorimetric measurements to assess binding affinities and discusses the implications of these findings for understanding cytokinin function and the broader roles of PR-10 proteins in plants.

Detailed Table of Contents:

• Introduction
• Materials and Methods (Protein production and purification, Crystallographic procedures, ITC, Antifungal assays)
• Results (Asymmetric unit contents, Model quality and overall folding, The binding cavity, The N- and C-termini, Structural comparisons of PR-10 proteins, Cytokinin-binding assays, Antifungal assays)
• Discussion
• Acknowledgements
• References