Yujia Zhai

Sichuan University

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Fei Sun

Institute of Biophysics

Xiaoyun Pang

Chinese Academy of Sciences

Milko A. Jorquera

Universidad de La Frontera

Junhong Bai

Australian National University

Ling Zhang

Tianjin University

Yaqi Wang

Jiangxi University of Traditional Chinese Medicine

Kegang Zhang

North China Electric Power University

Rong Xiao

Huazhong Agricultural University

Ruoxuan Tang

Beijing Normal University

Kai Zhang

Yale University

Cooperative Institutions

Chinese Academy of Sciences

University of Chinese Academy of Sciences

Institute of Biophysics

Beijing Normal University

State Key Joint Laboratory of Environment Simulation and Pollution Control

Czech Academy of Sciences, Institute of Biophysics

Institute of Genetics and Developmental Biology

Jilin University

Xiamen University

Fudan University

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Cryo-EM structure and electrophysiological characterization of ALMT from Glycine max reveal a previously uncharacterized class of anion channels

Science Advances (2022)

Qin Li Ling-hui Tang Jiashu Xu Xianhui Zhang Yun Zhu

Aluminum-activated malate transporters (ALMTs) form an anion channel family that plays essential roles in diverse functions in plants. Arabidopsis ALMT12, also named QUAC1 (quick anion channel 1), regulates stomatal closure in response to environmental stimuli. However, the molecular basis of ALMT12/QUAC1 activity remains elusive. Here, we describe the cryo-EM structure of ALMT12/QUAC1 from Glycine max at 3.5-Å resolution. GmALMT12/QUAC1 is a symmetrical dimer, forming a single electropositive T-shaped pore across the membrane. The transmembrane and cytoplasmic domains are assembled into a twisted two-layer architecture, with their associated dimeric interfaces nearly perpendicular. GmALMT12/QUAC1-mediated currents display rapid kinetics of activation/deactivation and a bell-shaped voltage dependency, reminiscent of the rapid (R)-type anion currents. Our structural and functional analyses reveal a domain-twisting mechanism for malate-mediated activation. Together, our study uncovers the molecular basis for a previously uncharacterized class of anion channels and provides insights into the gating and modulation of the ALMT12/QUAC1 anion channel.

10.1126/sciadv.abm3238

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Citations (19)

Multimedia distribution, partitioning, sources, comprehensive toxicity risk and co-occurrence network characteristics of trace elements in a typical Chinese shallow lake with high antibiotic risk

Journal of Hazardous Materials (2024)

Ling Zhang Junhong Bai Yujia Zhai Kegang Zhang Yaqi Wang

Trace element

10.1016/j.jhazmat.2024.133436

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Citations (2)

A cryo-electron microscopy support film formed by 2D crystals of hydrophobin HFBI

Nature Communications (2021)

Hongcheng Fan Bo Wang Yan Zhang Yun Zhu Bo Song

Abstract Cryo-electron microscopy (cryo-EM) has become a powerful tool to resolve high-resolution structures of biomacromolecules in solution. However, air-water interface induced preferred orientations, dissociation or denaturation of biomacromolecules during cryo-vitrification remains a limiting factor for many specimens. To solve this bottleneck, we developed a cryo-EM support film using 2D crystals of hydrophobin HFBI. The hydrophilic side of the HFBI film adsorbs protein particles via electrostatic interactions and sequesters them from the air-water interface, allowing the formation of sufficiently thin ice for high-quality data collection. The particle orientation distribution can be regulated by adjusting the buffer pH. Using this support, we determined the cryo-EM structures of catalase (2.29 Å) and influenza haemagglutinin trimer (2.56 Å), which exhibited strong preferred orientations using a conventional cryo-vitrification protocol. We further show that the HFBI film is suitable to obtain high-resolution structures of small proteins, including aldolase (150 kDa, 3.28 Å) and haemoglobin (64 kDa, 3.6 Å). Our work suggests that HFBI films may have broad future applications in increasing the success rate and efficiency of cryo-EM.

Hydrophobin

Cryo-Electron Microscopy

10.1038/s41467-021-27596-8

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Citations (32)

Correction: New interfaces on MiD51 for Drp1 recruitment and regulation

PLoS ONE (2019)

Jun Ma Yujia Zhai Ming Chen Kai Zhang Quan Chen

[This corrects the article DOI: 10.1371/journal.pone.0211459.].

10.1371/journal.pone.0217720

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Citations (3)

Ecological threshold effect mediates the long-term synergistic management of mega-city runoff nutrients in large-scale hybrid constructed wetlands

Chemical Engineering Journal (2024)

Baoshan Cui Guogui Chen Yuanyuan Mo Xinyu Li Xuan Gu

10.1016/j.cej.2024.154329

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Pollution levels and potential ecological risks of trace elements in relation to bacterial community in surface water of shallow lakes in northern China before and after ecological water replenishment

Journal of Contaminant Hydrology (2024)

Ling Zhang Junhong Bai Yujia Zhai Kegang Zhang Yaqi Wang

Functional ecology

TRACE (psycholinguistics)

Ecological health

10.1016/j.jconhyd.2024.104318

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Citations (4)

Spatial variability, source identification and risks assessment of antibiotics in multimedia of North China's largest freshwater lake using positive matrix factorization and Monte Carlo simulation

Journal of Hazardous Materials (2023)

Ling Zhang Junhong Bai Kegang Zhang Yujia Zhai Yaqi Wang

Health Risk Assessment

10.1016/j.jhazmat.2023.131751

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Crystal structure of E. coli apolipoprotein N-acyl transferase

Nature Communications (2017)

Guangyuan Lu Yingzhi Xu Kai Zhang Yong Xiong He Li

Abstract In Gram-negative bacteria, lipid modification of proteins is catalysed in a three-step pathway. Apolipoprotein N-acyl transferase (Lnt) catalyses the third step in this pathway, whereby it transfers an acyl chain from a phospholipid to the amine group of the N-terminal cysteine residue of the apolipoprotein. Here, we report the 2.6-Å crystal structure of Escherichia coli Lnt. This enzyme contains an exo-membrane nitrilase domain fused to a transmembrane (TM) domain. The TM domain of Lnt contains eight TM helices which form a membrane-embedded cavity with a lateral opening and a periplasmic exit. The nitrilase domain is located on the periplasmic side of the membrane, with its catalytic cavity connected to the periplasmic exit of the TM domain. An amphipathic lid loop from the nitrilase domain interacts with the periplasmic lipid leaflet, forming an interfacial entrance from the lipid bilayer to the catalytic centre for both the lipid donor and acceptor substrates.

Transferase

10.1038/ncomms15948

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Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIα

Nature Communications (2014)

Qiangjun Zhou Jiangmei Li Hang Yu Yujia Zhai Zhen Gao

Phosphatidylinositol 4-kinase IIα (PI4KIIα), a membrane-associated PI kinase, plays a central role in cell signalling and trafficking. Its kinase activity critically depends on palmitoylation of its cysteine-rich motif (-CCPCC-) and is modulated by the membrane environment. Lack of atomic structure impairs our understanding of the mechanism regulating kinase activity. Here we present the crystal structure of human PI4KIIα in ADP-bound form. The structure identifies the nucleotide-binding pocket that differs notably from that found in PI3Ks. Two structural insertions, a palmitoylation insertion and an RK-rich insertion, endow PI4KIIα with the ‘integral’ membrane-binding feature. Molecular dynamics simulations, biochemical and mutagenesis studies reveal that the palmitoylation insertion, containing an amphipathic helix, contributes to the PI-binding pocket and anchors PI4KIIα to the membrane, suggesting that fluctuation of the palmitoylation insertion affects PI4KIIα’s activity. We conclude from our results that PI4KIIα’s activity is regulated indirectly through changes in the membrane environment. Type II PI4-kinase dysfunction is associated with diseases including cancer and Alzheimer's disease; however, the development of specific modulators has been hampered by a lack of structural information. Zhou et al. present the crystal structure of PI4KIIα in its ADP-bound form, providing insight into its regulation.

Palmitoylation

HEK 293 cells

10.1038/ncomms4552

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Citations (54)

New interfaces on MiD51 for Drp1 recruitment and regulation

PLoS ONE (2019)

Jun Ma Yujia Zhai Ming Chen Kai Zhang Quan Chen

Mitochondrial fission is facilitated by dynamin-related protein Drp1 and a variety of its receptors. However, the molecular mechanism of how Drp1 is recruited to the mitochondrial surface by receptors MiD49 and MiD51 remains elusive. Here, we showed that the interaction between Drp1 and MiD51 is regulated by GTP binding and depends on the polymerization of Drp1. We identified two regions on MiD51 that directly bind to Drp1, and found that dimerization of MiD51, relevant to residue C452, is required for mitochondrial dynamics regulation. Our Results have suggested a multi-faceted regulatory mechanism for the interaction between Drp1 and MiD51 that illustrates the potentially complicated and tight regulation of mitochondrial fission.

DNM1L

10.1371/journal.pone.0211459

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Citations (17)