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Instruments / Technical Area	Publication Details	Published	Actions
I24-Microfocus Macromolecular Crystallography	Structural insights into the human niacin receptor HCA2-Gi signalling complex Yang Yang , Hye Jin Kang , Ruogu Gao , Jingjing Wang , Gye Won Han , Jeffrey F. Diberto , Lijie Wu , Jiahui Tong , Lu Qu , Yiran Wu , Ryan Pileski , Xuemei Li , Xuejun Cai Zhang , Suwen Zhao , Terry Kenakin , Quan Wang , Raymond C. Stevens , Wei Peng , Bryan L. Roth , Zihe Rao , Zhi-Jie Liu Nature Communications 14 DOI: 10.1038/s41467-023-37177-6 Open Access Show Abstract ▼ Abstract: The hydroxycarboxylic acid receptor 2 (HCA2) agonist niacin has been used as treatment for dyslipidemia for several decades albeit with skin flushing as a common side-effect in treated individuals. Extensive efforts have been made to identify HCA2 targeting lipid lowering agents with fewer adverse effects, despite little being known about the molecular basis of HCA2 mediated signalling. Here, we report the cryo-electron microscopy structure of the HCA2-Gi signalling complex with the potent agonist MK-6892, along with crystal structures of HCA2 in inactive state. These structures, together with comprehensive pharmacological analysis, reveal the ligand binding mode and activation and signalling mechanisms of HCA2. This study elucidates the structural determinants essential for HCA2 mediated signalling and provides insights into ligand discovery for HCA2 and related receptors.	Mar 2023
I04-1-Macromolecular Crystallography (fixed wavelength)	Structures of cell wall arabinosyltransferases with the anti-tuberculosis drug ethambutol Lu Zhang , Yao Zhao , Yan Gao , Lijie Wu , Ruogu Gao , Qi Zhang , Yinan Wang , Chengyao Wu , Fangyu Wu , Sudagar S. Gurcha , Natacha Veerapen , Sarah M. Batt , Wei Zhao , Ling Qin , Xiuna Yang , Manfu Wang , Yan Zhu , Bing Zhang , Lijun Bi , Xian’en Zhang , Haitao Yang , Luke W. Guddat , Wenqing Xu , Quan Wang , Jun Li , Gurdyal S. Besra , Zihe Rao Science 4 DOI: 10.1126/science.aba9102 Show Abstract ▼ Abstract: The arabinosyltransferases EmbA, EmbB, and EmbC are involved in Mycobacterium tuberculosis cell wall synthesis and are recognized as the targets for the anti-tuberculosis drug ethambutol. We have determined cryo-electron microscopy and x-ray crystal structures of mycobacterial EmbA-EmbB and EmbC-EmbC complexes, in the presence of their glycosyl donor and acceptor substrates and with ethambutol. These structures show how the donor and acceptor substrates bind in the active site and how ethambutol inhibits by binding to the same site as both substrates in EmbB and EmbC. The majority of drug-resistant mutations are located nearby to the ethambutol-binding site. Collectively, our work provides a structural basis for understanding the biochemical function and inhibition of arabinosyltransferases and development of new anti-tuberculosis agents.	Apr 2020

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