5MXW

Crystal structure of yellow lupin LLPR-10.2B protein in complex with melatonin and trans-zeatin.

Summary for 5MXW

• Entry DOI: 10.2210/pdb5mxw/pdb
• Related: 1icx 1ifv 1xdf 2flh 2qim 3e85 3ie5 4gy9 4jhg 4jhh 4jhi 4n3e 4psb 4q0k 4ryv 4y31 5c9y 5mxb
• Descriptor: Class 10 plant pathogenesis-related protein, UNKNOWN LIGAND, SODIUM ION, ... (6 entities in total)
• Functional Keywords: plant protein, phytohormon binding protein, pr-10 protein, melatonin
• Biological source: Lupinus luteus (European yellow lupine)
• Total number of polymer chains: 1
• Total formula weight: 17135.21

Authors

Sliwiak, J.,Sikorski, M.,Jaskolski, M. (deposition date: 2017-01-25, release date: 2018-04-18, Last modification date: 2024-01-17)

Primary citation

Sliwiak, J.,Sikorski, M.,Jaskolski, M.
PR-10 proteins as potential mediators of melatonin-cytokinin cross-talk in plants: crystallographic studies of LlPR-10.2B isoform from yellow lupine.
FEBS J., 285:1907-1922, 2018

PubMed Abstract: LlPR-10.2B, a Pathogenesis-related class 10 (PR-10) protein from yellow lupine (Lupinus luteus) was crystallized in complex with melatonin, an emerging important plant regulator and antioxidant. The structure reveals two molecules of melatonin bound in the internal cavity of the protein, plus a very well-defined electron density near the cavity entrance, corresponding to an unknown ligand molecule comprised of two flat rings, which is most likely a product of melatonin transformation. In a separate LlPR-10.2B co-crystallization experiment with an equimolar mixture of melatonin and trans-zeatin, which is a cytokinin phytohormone well recognized as a PR-10-binding partner, a quaternary 1 : 1 : 1 : 1 complex was formed, in which one of the melatonin-binding sites has been substituted with trans-zeatin, whereas the binding of melatonin at the second binding site and binding of the unknown ligand are undisturbed. This unusual complex, when compared with the previously described PR-10/trans-zeatin complexes and with the emerging structural information about melatonin binding by PR-10 proteins, provides intriguing insights into the role of PR-10 proteins in phytohormone regulation in plants, especially with the involvement of melatonin, and implicates the PR-10 proteins as low-affinity melatonin binders under the conditions of elevated melatonin concentration.

PubMed: 29630775
DOI: 10.1111/febs.14455

Experimental method

X-RAY DIFFRACTION (1.57 Å)