4JHG

Crystal Structure of Medicago truncatula Nodulin 13 (MtN13) in complex with trans-zeatin

Replaces:  3RWS

Summary for 4JHG

• Entry DOI: 10.2210/pdb4jhg/pdb
• Related: 1icx 2qim 3us7 4JHH 4JHI 4gy9
• Descriptor: MtN13 protein, (2E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol, MALONATE ION, ... (5 entities in total)
• Functional Keywords: pr-10 fold, nodulin, nodulation, legume-bacteria symbiosis, nitrogen fixation, cytokinin binding, plant protein
• Biological source: Medicago truncatula (Barrel medic)
• Total number of polymer chains: 1
• Total formula weight: 19163.28

Authors

Ruszkowski, M.,Tusnio, K.,Ciesielska, A.,Brzezinski, K.,Dauter, M.,Dauter, Z.,Sikorski, M.,Jaskolski, M. (deposition date: 2013-03-05, release date: 2013-03-20, Last modification date: 2023-09-20)

Primary citation

Ruszkowski, M.,Szpotkowski, K.,Sikorski, M.,Jaskolski, M.
The landscape of cytokinin binding by a plant nodulin.
Acta Crystallogr.,Sect.D, 69:2365-2380, 2013

PubMed Abstract: Nodulation is an extraordinary symbiotic interaction between leguminous plants and nitrogen-fixing bacteria (rhizobia) that assimilate atmospheric nitrogen (in root nodules) and convert it into compounds suitable for the plant host. A class of plant hormones called cytokinins are involved in the nodulation process. In the model legume Medicago truncatula, nodulin 13 (MtN13), which belongs to the pathogenesis-related proteins of class 10 (PR-10), is expressed in the outer cortex of the nodules. In general, PR-10 proteins are small and monomeric and have a characteristic fold with an internal hydrophobic cavity formed between a seven-stranded antiparallel β-sheet and a C-terminal α-helix. Previously, some PR-10 proteins not related to nodulation were found to bind cytokinins such as trans-zeatin. Here, four crystal structures of the MtN13 protein are reported in complexes with several cytokinins, namely trans-zeatin, N6-isopentenyladenine, kinetin and N6-benzyladenine. All four phytohormones are bound in the hydrophobic cavity in the same manner and have excellent definition in the electron-density maps. The binding of the cytokinins appears to be strong and specific and is reinforced by several hydrogen bonds. Although the binding stoichiometry is 1:1, the complex is actually dimeric, with a cytokinin molecule bound in each subunit. The ligand-binding site in each cavity is formed with the participation of a loop element from the other subunit, which plugs the only entrance to the cavity. Interestingly, a homodimer of MtN13 is also formed in solution, as confirmed by small-angle X-ray scattering (SAXS).

PubMed: 24311578
DOI: 10.1107/S0907444913021975

Experimental method

X-RAY DIFFRACTION (1.85 Å)