Steffen Brünle
Assistant Professor
- Name
- Dr. S. Brünle
- Telephone
- +31 71 527 4544
- s.bruenle@lic.leidenuniv.nl
Steffen Brünle investigates the structural details of GPCRs and is particularly interested in allosteric modulation, biased signaling, and drug discovery. He uses single-particle cryo-EM, as well as classical and time-resolved X-ray crystallography at synchrotrons and free electron lasers to unravel structural snapshots and dynamics of proteins.
Biography
Steffen Brünle was born in Darmstadt, Germany; he completed his studies in "Molecular Biology with emphasis on Human and Molecular Biology" at Saarland University in 2012 and finished his diploma thesis in the Department of Structural Biology investigating membrane proteins from anaerobic bacteria under the supervision of Prof. Roy Lancaster. Steffen Brünle received a Fellowship from the International Max-Planck Research School to start his doctoral studies at the Max Plank Institute of Biophysics in Frankfurt, Germany.
In the Department of Molecular Membrane Biology (Prof. Dr. Dr. h.c. Hartmut Michel), Steffen Brünle worked in the group of Dr. Ulrich Ermler on a soluble metal-containing protein using methods in molecular biology, biochemistry and biophysics, including classical X-ray crystallography and single-particle cryo-electron microscopy. After completing his Ph.D. Steffen Brünle secured a Marie-Curie CoFund Fellowship and started his postdoctoral studies at the Paul Scherrer Institute, Villigen, Switzerland in the BIO Division (Prof. Dr. Gebhard Schertler) within the group of Dr. Jörg Standfuss.
Steffen Brünle used time-resolved X-ray crystallography using synchrotron radiation and free-electron lasers to study the structural dynamics of retinal proteins. Besides his work in time-resolved crystallography, Steffen worked on the structural elucidation and characterization of the human GPCR Chemokine Receptor 7. In collaboration with the pharmaceutical company Roche, the team solved the structure of CCR7 and identified small molecule that binds to a novel allosteric site on the receptor (Jaeger, K. & Bruenle, S. et al. Cell 178, 1222–1230.e10 (2019)).
During his postdoctoral studies Steffen Brünle secured a Spark Grant from the Swiss National Science Foundation to uncover a novel regulatory concept for GPCRs that he developed. In 2020 Steffen was invited to speak at the Lindau Nobel Laureate Meetings in the NextGen Science session, in which scientific talents showcase their research.
In 2021 Steffen Brünle is appointed assistant professor at the Biophysical Structural Chemistry Department within the Leiden Institute of Chemistry at Leiden University.
Assistant Professor
- Science
- Leiden Institute of Chemistry
- LIC/Chemical Biology
- LIC/CB/Biophysical Structural Chemistry
- Alen I. van, Chikunova A., Zanten D.B. van, Block A.A. de, Timmer M., Brünle S. & Ubbink M. (2023), Asp179 in the class A β‐lactamase from Mycobacterium tuberculosis is a conserved yet not essential residue due to epistasis, FEBS Journal 290: 4933-4949.
- Mous S., Gotthard G., Ehrenberg D., Sen S., Weinert T., Johnson P.J.M., James D., Nass K., Furrer A., Kekilli D., Ma P., Brunle S., Casadei C.M., Martiel I., Dworkowski F., Gashi D., Skopintsev P., Wranik M., Knopp G., Panepucci E., Panneels V., Cirelli C., Ozerov D., Schertler G.F.X., Wang M.T., Milne C., Standfuss J., Schapiro I., Heberle J. & Nogly P. (2022), Dynamics and mechanism of a light-driven chloride pump, Science 375(6583): 845-851.
- Skopintsev P., Ehrenberg D., Weinert T., James D., Kar R.K, Johnson P.J.M., Ozerov D., Furrer A., Martiel I., Dworkowski F., Nass K., Knopp G., Cirelli C., Arrell C., Gashi D., Mous S., Wranik M., Gruhl T., Kekilli D., Brünle S., Deupi X., Schertler G.F.X., Benoit R.M., Panneels V., Nogly P., Schapiro I., Milne C., Heberle J. & Standfuss J. (2020), Femtosecond-to-millisecond structural changes in a light-driven sodium pump, NATURE 583: 314-318.
- Jaeger K., Bruenle S., Weinert T., Guba W., Muehle J., Miyazaki T., Weber M., Furrer A., Haenggi N., Tetaz T., Huang C.Y., Mattle D., Vonach J.M., Gast A., Kuglstatter A., Rudolph M.G., Nogly P., Benz J., Dawson R.J.P. & Standfuss J. (2019), Structural Basis for Allosteric Ligand Recognition in the Human CC Chemokine Receptor 7, Cell 178(5): 1222-1230e10.
- Brünle S., Eisinger M.L., Poppe J., Mills D.J., Langer J.D., Vonck J. & Ermler U. (2019), Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism, Proceedings of the National Academy of Sciences 116(52): 26497-26504.
- Weinert T., Skopintsev P., James D., Dworkowski F., Panepucci E., Kekilli D., Furrer A., Brünle S., Mous S., Ozerov D., Nogly P., Wang M. & Standfuss J. (2019), Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography, Science 365(6448): 61-65.
- Nogly P., Weinert T., James D., Carbajo S., Ozerov D., Furrer A., Gashi D., Borin V., Skopintsev P., Jaeger K., Nass K., Båth P., Bosman R., Koglin J., Seaberg M., Lane T., Kekilli D., Brünle S., Tanaka T., Wu W., Milne C., White T., Barty A. Weierstall U., Panneels V., Nango E., Iwata S., Hunter M., Schapiro I., Schertler G., Neutze R. & Standfuss J. (2018), Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser, Science 361(6398).
- Poppe J., Brünle S., Hail R., Wiesemann K., Schneider K. & Ermler U. (2018), The Molybdenum Storage Protein: A solubleATPhydrolysis‐dependent molybdate pump, FEBS Journal 285: 4602-4616.
- Brünle S., Poppe J., Hail R., Demmer U. & Ermler U. (2018), The molybdenum storage protein — A bionanolab for creating experimentally alterable polyoxomolybdate clusters, Journal of Inorganic Biochemistry 189: 172-179.
- Weinert T., Olieric N., Cheng R., Brünle S., James D., Ozerov D., Gashi D., Vera L., Marsh M., Jaeger K., Dworkowski F., Panepucci E., Basu S., Skopintsev P., Doré A.S., Geng T., Cooke R.M., Liang M., Prota A.E., Panneels V., Nogly P., Ermler U., Schertler G., Hennig M., Steinmetz M.O., Wang M. & Standfuss J. (2017), Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons, Nature Communications 8: 542.
- Konjik V., Brünle S., Demmer U., Vanselow A., Sandhoff R., Ermler U. & Mack M. (2016), The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes, Angewandte Chemie - International Edition in English 56(4): 1146-1151.
- Konjik V., Brünle S., Demmer U., Vanselow A., Sandhoff R., Ermler U. & Mack M. (2016), Die Kristallstruktur von RosB: Einblicke in den Reaktionsmechanismus des ersten Mitglieds einer flavodoxinähnlichen Enzymfamilie, Angewandte Chemie 129(4): 1166-1171.