XFEL and NMR Structures of Francisella Lipoprotein Reveal Conformational Space of Drug Target against Tularemia

• Published in: Structure (London) Vol. 28; no. 5
• Main Authors: Zook, James, Shekhar, Mrinal, Hansen, Debra, Conrad, Chelsie, Grant, Thomas, Gupta, Chitrak, White, Thomas, Barty, Anton, Basu, Shibom, Zhao, Yun, Zatsepin, Nadia, Ishchenko, Andrii, Batyuk, Alex, Gati, Cornelius, Li, Chufeng, Galli, Lorenzo, Coe, Jesse, Hunter, Mark, Liang, Meng, Weierstall, Uwe, Nelson, Garret, James, Daniel, Stauch, Benjamin, Craciunescu, Felicia, Thifault, Darren, Liu, Wei, Cherezov, Vadim, Singharoy, Abhishek, Fromme, Petra
• Format: Journal Article
• Language: English
• Published: United Kingdom Elsevier 01.05.2020
• Subjects: BASIC BIOLOGICAL SCIENCES; computational chemistry; drug discovery; Francisella tularensis; intergrative modeling; molecular biophysics; NMR spectroscopy; serial femtosecond crystallography; X-ray crystallography

Francisella tularensis is the causative agent for the potentially fatal disease tularemia. The lipoprotein Flpp3 has been identified as a virulence determinant of tularemia with no sequence homology outside the Francisella genus. We report a room temperature structure of Flpp3 determined by serial f...