7wst
From Proteopedia
Cryo-EM structure of the barley Yellow stripe 1 transporter in complex with Fe(III)-DMA
Structural highlights
FunctionPublication Abstract from PubMedCalcareous 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 beta-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. Uptake mechanism of iron-phytosiderophore from the soil based on the structure of yellow stripe transporter.,Yamagata A, Murata Y, Namba K, Terada T, Fukai S, Shirouzu M Nat Commun. 2022 Nov 23;13(1):7180. doi: 10.1038/s41467-022-34930-1. PMID:36424382[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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