7WST
Cryo-EM structure of the barley Yellow stripe 1 transporter in complex with Fe(III)-DMA
Summary for 7WST
Entry DOI | 10.2210/pdb7wst/pdb |
EMDB information | 32766 |
Descriptor | Iron-phytosiderophore transporter, CHOLESTEROL HEMISUCCINATE, FE (III) ION, ... (4 entities in total) |
Functional Keywords | iron-phytosiderophore transporter, deoxymugineic acid, metal transport |
Biological source | Hordeum vulgare |
Total number of polymer chains | 2 |
Total formula weight | 154809.15 |
Authors | Yamagata, A. (deposition date: 2022-02-01, release date: 2022-11-30, Last modification date: 2024-11-06) |
Primary citation | Yamagata, A.,Murata, Y.,Namba, K.,Terada, T.,Fukai, S.,Shirouzu, M. Uptake mechanism of iron-phytosiderophore from the soil based on the structure of yellow stripe transporter. Nat Commun, 13:7180-7180, 2022 Cited by PubMed Abstract: Calcareous soils cover one-third of all land and cause severe growth defects in plants due to the poor water solubility of iron at high pH. Poaceae species use a unique chelation strategy, whereby plants secrete a high-affinity metal chelator, known as phytosiderophores (mugineic acids), and reabsorb the iron-phytosiderophore complex by the yellow stripe 1/yellow stripe 1-like (YS1/YSL) transporter for efficient uptake of iron from the soil. Here, we present three cryo-electron microscopy structures of barley YS1 (HvYS1) in the apo state, in complex with an iron-phytosiderophore complex, Fe(III)-deoxymugineic acid (Fe(III)-DMA), and in complex with the iron-bound synthetic DMA analog (Fe(III)-PDMA). The structures reveal a homodimeric assembly mediated through an anti-parallel β-sheet interaction with cholesterol hemisuccinate. Each protomer adopts an outward open conformation, and Fe(III)-DMA is bound near the extracellular space in the central cavity. Fe(III)-PDMA occupies the same binding site as Fe(III)-DMA, demonstrating that PDMA can function as a potent fertilizer in an essentially identical manner to DMA. Our results provide a structural framework for iron-phytosiderophore recognition and transport by YS1/YSL transporters, which will enable the rational design of new, high-potency fertilizers. PubMed: 36424382DOI: 10.1038/s41467-022-34930-1 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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