8WO7
Apo state of Arabidopsis AZG1 T440Y
Summary for 8WO7
Entry DOI | 10.2210/pdb8wo7/pdb |
EMDB information | 37681 |
Descriptor | Adenine/guanine permease AZG1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
Functional Keywords | transport protein |
Biological source | Arabidopsis thaliana (thale cress) |
Total number of polymer chains | 2 |
Total formula weight | 132346.35 |
Authors | |
Primary citation | Xu, L.,Jia, W.,Tao, X.,Ye, F.,Zhang, Y.,Ding, Z.J.,Zheng, S.J.,Qiao, S.,Su, N.,Zhang, Y.,Wu, S.,Guo, J. Structures and mechanisms of the Arabidopsis cytokinin transporter AZG1. Nat.Plants, 10:180-191, 2024 Cited by 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 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. PubMed: 38172575DOI: 10.1038/s41477-023-01590-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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