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-Structure paper
Title | Structural insights into auxin recognition and efflux by Arabidopsis PIN1. |
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Journal, issue, pages | Nature, Vol. 609, Issue 7927, Page 611-615, Year 2022 |
Publish date | Aug 2, 2022 |
Authors | Zhisen Yang / Jing Xia / Jingjing Hong / Chenxi Zhang / Hong Wei / Wei Ying / Chunqiao Sun / Lianghanxiao Sun / Yanbo Mao / Yongxiang Gao / Shutang Tan / Jiří Friml / Dianfan Li / Xin Liu / Linfeng Sun / |
PubMed Abstract | Polar auxin transport is unique to plants and coordinates their growth and development. The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and ...Polar auxin transport is unique to plants and coordinates their growth and development. The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and drive polar auxin transport; however, their structures and transport mechanisms remain largely unknown. Here, we report three inward-facing conformation structures of Arabidopsis thaliana PIN1: the apo state, bound to the natural auxin indole-3-acetic acid (IAA), and in complex with the polar auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). The transmembrane domain of PIN1 shares a conserved NhaA fold. In the substrate-bound structure, IAA is coordinated by both hydrophobic stacking and hydrogen bonding. NPA competes with IAA for the same site at the intracellular pocket, but with a much higher affinity. These findings inform our understanding of the substrate recognition and transport mechanisms of PINs and set up a framework for future research on directional auxin transport, one of the most crucial processes underlying plant development. |
External links | Nature / PubMed:35917925 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.1 - 3.3 Å |
Structure data | EMDB-33691, PDB-7y9t: EMDB-33692, PDB-7y9u: EMDB-33693, PDB-7y9v: |
Chemicals | ChemComp-E7O: ChemComp-IAC: ChemComp-HOH: |
Source |
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Keywords | TRANSPORT PROTEIN |