Volume 32, No 1, Jan 2022

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 32 Issue 1, January 2022: 89-98

ORIGINAL ARTICLES

Structural basis of ALMT1-mediated aluminum resistance in Arabidopsis

Jiangqin Wang^1,† , Xiafei Yu^2,† , Zhong Jie Ding^3,† , Xiaokang Zhang^4,5,† , Yanping Luo² , Ximing Xu⁶ , Yuan Xie¹ , Xiaoxiao Li¹ , Tian Yuan³ , Shao Jian Zheng^3,* , Wei Yang^2,* , Jiangtao Guo^1,3,7,8,9,*

¹Department of Biophysics, and Department of Pathology of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China
²Department of Biophysics and Department of Neurosurgery, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China
³State Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, China
⁴Interdisciplinary Center for Brain Information, The Brain Cognition and Brain Disease Institute, Faculty of Life and Health Sciences, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen, Guangdong, China
⁵ShenzhenHong Kong Institute of Brain Science-Shenzhen Fundamental Research Institutions, Shenzhen, Guangdong, China
⁶Key Laboratory of Marine Drugs of Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao, Shandong, China
⁷Department of Cardiology, Key Laboratory of Cardiovascular Intervention and Regenerative Medicine of Zhejiang Province, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China
⁸Cancer Center, Zhejiang University, Hangzhou, Zhejiang, China
⁹Liangzhu Laboratory, Zhejiang University Medical Center, 1369 West Wenyi Road, Hangzhou, Zhejiang, China
^†These authors contributed equally: Jiangqin Wang, Xiafei Yu, Zhong Jie Ding, Xiaokang Zhang
Correspondence: Shao Jian Zheng(sjzheng@zju.edu.cn)Wei Yang(yangwei@zju.edu.cn)Jiangtao Guo(jiangtaoguo@zju.edu.cn)

The plant aluminum (Al)-activated malate transporter ALMT1 mediates the efflux of malate to chelate the Al in acidic soils and underlies the plant Al resistance. Here we present cryo-electron microscopy (cryo-EM) structures of Arabidopsis thaliana ALMT1 (AtALMT1) in the apo, malate-bound, and Al-bound states at neutral and/or acidic pH at up to 3.0 Å resolution. The AtALMT1 dimer assembles an anion channel and each subunit contains six transmembrane helices (TMs) and six cytosolic α-helices. Two pairs of Arg residues are located in the center of the channel pore and contribute to malate recognition. Al binds at the extracellular side of AtALMT1 and induces conformational changes of the TM1–2 loop and the TM5–6 loop, resulting in the opening of the extracellular gate. These structures, along with electrophysiological measurements, molecular dynamic simulations, and mutagenesis study in Arabidopsis, elucidate the structural basis for Al-activated malate transport by ALMT1.

https://doi.org/10.1038/s41422-021-00587-6

FULL TEXT | PDF

Browse 705