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-Structure paper
Title | Structures and mechanisms of the Arabidopsis cytokinin transporter AZG1. |
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Journal, issue, pages | Nat Plants, Vol. 10, Issue 1, Page 180-191, Year 2024 |
Publish date | Jan 3, 2024 |
Authors | Lingyi Xu / Wei Jia / Xin Tao / Fan Ye / Yan Zhang / Zhong Jie Ding / Shao Jian Zheng / Shuai Qiao / Nannan Su / Yu Zhang / Shan Wu / Jiangtao Guo / |
PubMed Abstract | Cytokinins are essential for plant growth and development, and their tissue distributions are regulated by transmembrane transport. Recent studies have revealed that members of the 'Aza-Guanine ...Cytokinins are essential for plant growth and development, and their tissue distributions are regulated by transmembrane transport. Recent studies have revealed that members of the 'Aza-Guanine Resistant' (AZG) protein family from Arabidopsis thaliana can mediate cytokinin uptake in roots. Here we present 2.7 to 3.3 Å cryo-electron microscopy structures of Arabidopsis AZG1 in the apo state and in complex with its substrates trans-zeatin (tZ), 6-benzyleaminopurine (6-BAP) or kinetin. AZG1 forms a homodimer and each subunit shares a similar topology and domain arrangement with the proteins of the nucleobase/ascorbate transporter (NAT) family. These structures, along with functional analyses, reveal the molecular basis for cytokinin recognition. Comparison of the AZG1 structures determined in inward-facing conformations and predicted by AlphaFold2 in the occluded conformation allowed us to propose that AZG1 may carry cytokinins across the membrane through an elevator mechanism. |
External links | Nat Plants / PubMed:38172575 |
Methods | EM (single particle) |
Resolution | 2.6 - 3.3 Å |
Structure data | EMDB-35678, PDB-8irl: EMDB-35679, PDB-8irm: EMDB-35680, PDB-8irn: EMDB-35681, PDB-8iro: EMDB-35682, PDB-8irp: EMDB-37658, PDB-8wmq: EMDB-37681, PDB-8wo7: |
Chemicals | ChemComp-ADE: ChemComp-HOH: ChemComp-EMU: ChemComp-ZEA: ChemComp-H35: |
Source |
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Keywords | TRANSPORT PROTEIN / cytokinin / transporter |