Assistant Scientist, Molecular and Cellular Biochemistry Department
Office: Simon Hall 200C
Indiana University Department of Neuroscience
B.S. 2003 University of Mainz (Germany)-Biology
M.S. 2006 University of Mainz (Germany) Honors Thesis at the Max-Planck
Institute of Biophysics-Biophysics, Immunology,
Ph.D. 2009 Max-Planck Institute of Biophysics (University of Frankfurt)
2010-2014 Postdoctoral Fellow at Stanford University CA with Axel T. Brunger - Structural Neuroscience
2010-2011 EMBO Longterm Fellowship
2012-2014 Otto-Hahn Fellowship of the Max-Planck Society Germany
Structure Biology allows us to look and analyze a protein’s three-dimensional structure and defer functional information from it. Biochemistry allows us to analyze a protein’s chemical properties and its physiological relevance on a chemical level. The powerful combination of both advances our understanding of molecular mechanisms of protein machineries on an atomic level. Solving the structure - function relationship of a protein enables the discovery of unexpected relationships between different protein families and can aid in the design of therapeutic strategies.
The Ressl lab focuses on solving protein structures, in particular membrane proteins. Membrane proteins are a fascinating class of proteins. Embedded in the cell’s membrane, they are the vital link between outside and inside world and facilitate various crucial physiological functions. Functions such as: 1) transporters, transporting molecules or ions across the membrane, 2) anchors, anchoring proteins and providing cell stability and interacting with cell matrix proteins, 3) receptors and enzyme that provide major signalling functions in the cell, such as G-protein coupled receptors that are involved in the majority of physiological functions.
Membrane proteins are involved in all aspects of physiological processes, therefore it is not surprising that about 40% of our genome encodes for membrane proteins. However, compared to the number of crystal structures of soluble proteins (~72000), membrane protein structures (~310) are underrepresented in the structure database.
The Ressl lab seeks to solve crystal structures of membrane protein targets that will increase our understanding of mechanisms of: a) ion and small molecule transport, b) cell adhesion and signaling and c) regulation of membrane lipid compositions in bacterial and mammalian systems. We also work on method development in membrane protein X-ray crystallography.
Sunden F., Peck A., Salzman J., Ressl S., Herschlag D. (2015) "Extensive site-directed mutagenesis reveals interconnected functional units in the Alkaline Phosphatase active site” eLife Sciences 04
Dalebroux Z.D., Edrozo M.B., Pfuetzner R.A., Ressl S., Kulasekara B.R., Blanc MP., Miller S.I. (2015) "Delivery of Cardiolipins to the Salmonella Outer Membrane Is Necessary for Survival within Host Tissues and Virulence” Cell Host & Microbe 17, 1–11, April 8, 2015
Zhang Y, Diao J, Colbert KN, Lai Y, Pfuetzner RA, Padolina MS, Vivona S, Ressl S, Cipriano DJ, Choi UB, Shah N, Weis WI, Brunger AT. (2015) "Munc18a does not alter fusion rates mediated by neuronal SNAREs, synaptotagmin, and complexin.” J Biol Chem. 2015 Feb 25.
Ressl S, Vu BK, Vivona S, Martinelli DC, Südhof TC, Brunger AT (2015) “Structures of C1q-like proteins reveal unique features among the C1q/TNF superfamily” STRUCTURE 2015 Feb 24
Liebscher I, Ackley B,[......], Ressl S, Schiöth HB, Sigoillot SM, Song H, Talbot WS, Tall GG, White JP, Wolfrum U, Xu L, Piao X (2014) “New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors” Annals of the New York Academy of Sciences 11/2014
Korkmaz F, Ressl S, Ziegler C, Mäntele W (2013) “K(+)-induced conformational changes in the trimeric betaine transporter BetP monitored by ATR-FTIR spectroscopy” Biochimica et Biophysica Acta 1828: 1181-1191
Perez C, Koshy C, Ressl S, Nicklisch S, Krämer R, Ziegler C (2011) “Substrate specificity and ion coupling in the Na+/betaine symporter BetP” The EMBO Journal 30:1221-9
Kraemer R, Ressl S, Ott V, Nicklisch S, Steinhoff HJ, Forrest L, Ziegler C (2010)”Betp - X-Ray Structure and Function of An Osmosensor and Transporter” Biophysical Journal 98(3)
Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V., Ziegler C (2009) “Molecular basis of transport and regulation in the Na+/betaine symporter BetP”Nature 458: 47-52