4jhg

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

spinqualitylabelsall models 4jhg, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jhg is a 1 chain structure with sequence from Medicago truncatula. This structure supersedes the now removed PDB entry 3rws. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: MLI, NA, ZEA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NOD13_MEDTR May be involved in nodule organogenesis rather in the processes related to nitrogen fixation or interactions with the bacteria. May regulate nodulation by controlling the levels of freely available cytokinins. Publication Abstract from PubMed 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 beta-sheet and a C-terminal alpha-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, N(6)-isopentenyladenine, kinetin and N(6)-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). The landscape of cytokinin binding by a plant nodulin.,Ruszkowski M, Szpotkowski K, Sikorski M, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2365-80. doi:, 10.1107/S0907444913021975. Epub 2013 Nov 19. PMID:24311578 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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