Structure of metalloproteins, membrane proteins, filamentous sarcomer proteins, and virus particles

Our work focusses on biological nitrogen fixation by Nitrogenase, on metalloenzymes and integral membrane proteins of bacterial and archaeal respiratory systems (Andrade/Einsle/Wohlwend), the working mechanism and regulation of medically relevant membrane proteins and complexes and their defects leading to pathologies (Hunte), bacterial antibiotic resistance factors and viral and bacterial proteins bound to their targets or inhibitors, and their interactions with glycans (Stehle/Zocher), human S100 proteins involved in nutritional immunity, USP18 enforcing the endogenous antiviral interferon response, and the respiratory complex NQR of V. cholerae (Fritz), DNA Polymerases with artificial substrates (Benz), and on multi-domain components of the sarcomeric filamentous protein titin and their binding to the E3 ubiquitin ligase MuRF1 and the central myosin rod-domain (Mayans).

我们的研究聚焦于固氮酶（Nitrogenase）介导的生物固氮作用、细菌与古菌呼吸系统中的金属酶及整合膜蛋白（Andrade/Einsle/Wohlwend团队）、具有医学意义的膜蛋白与复合物的工作机制、调控方式及其缺陷引发疾病的机制（Hunte团队）、细菌抗生素耐药性因子、结合于靶标或抑制剂的病毒与细菌蛋白及其与聚糖的相互作用（Stehle/Zocher团队）、参与营养免疫的人类S100蛋白、增强内源性抗病毒干扰素应答的USP18以及霍乱弧菌（V. cholerae）的呼吸复合物NQR（Fritz团队）、使用人工底物的DNA聚合酶（Benz团队），以及肌节丝状蛋白肌联蛋白（titin）的多结构域组分及其与E3泛素连接酶MuRF1和肌球蛋白中央杆状结构域的结合作用（Mayans团队）。