Research interests

  • elucidating molecular details and mechanisms of signal transduction processes in membrane proteins (e.g., G-protein-coupled receptors), signal transduction-related proteins (e.g., arrestin, phosphodiesterase), photoreceptors (e.g., phytochromes, opsins) and metalloenzymes (e.g., [NiFe]-hydrogenases)

  • protein X-ray crystallography, molecular biology/protein production methods, biophysical assays (e.g. MST/nanoDSF/Nanodiscs/SMALPs), LCP crystallisation, free-electron laser techniques, cryo-electron microscopy (in cooperation)

Dr. Patrick Scheerer
Charité – Universitätsmedizin
Institute of Medical Physics and Biophysics
Protein X-ray Crystallography & Signal Transduction
Charitéplatz 1
10117 Berlin
+49 (0)30 450 524 178
+49 (0)30 450 524 952
patrick.scheerer(at)charite.de
https://biophysik.charite.de/scheerer

UniSysCat Publications

  • Design of a light-gated proton channel based on the crystal structure of Coccomyxa rhodopsin, R. Fudim, M. Szczepek, J. Vierock, A. Vogt, A. Schmidt, G. Kleinau, P. Fischer, F. Bartl, P. Scheerer, P. Hegemann, Science Signaling 2019, 12, 10.1126/scisignal.aav4203

Publications (selection)

A. Schmidt, L. Sauthof, M. Szczepek, M. F. Lopez, F. V. Escobar, B. M. Qureshi, N. Michael, D. Buhrke, T. Stevens, D. Kwiatkowski, D. von Stetten, M. A. Mroginski, N. Krauß, T. Lamparter, P. Hildebrandt, P. Scheerer, Structural snapshot of a bacterial phytochrome in its functional intermediate state. Nature Communications  2018, 9(1), 4912.

J. Kalms, A. Schmidt, S. Frielingsdorf, T. Utesch, G. Gotthard, D. von Stetten, P. van der Linden, A. Royant, M. A. Mroginski, P. Carpentier, O. Lenz, P. Scheerer, Tracking the route of molecular oxygen in O2-tolerant membrane-bound [NiFe] hydrogenase. Proc Natl Acad Sci U S A.  2018, 115(10), E2229-E2237.

B. M. Qureshi, A. Schmidt, E. Behrmann, J. Bürger, T. Mielke, C. M. T. Spahn, M. Heck, P. Scheerer, Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6, Nature Communications  2018, 9(1), 90.

M. Szczepek, F. Beyrière, K. P. Hofmann, M. Elgeti, R. Kazmin, A. Rose, F. J. Bartl, D. von Stetten, M. Heck, M. E. Sommer, P. W. Hildebrand, P. Scheerer, Crystal structure of a common GPCR binding interface for G protein and arrestin, Nature Communications 2014, 5, 4801.

S. Frielingsdorf, J. Fritsch, A. Schmidt, M. Hammer, J. Löwenstein, E. Siebert, V. Pelmenschikov, T. Jaenicke, J. Kalms, Y. Rippers, F. Lendzian, I. Zebger, C. Teutloff, M. Kaupp, R. Bittl, P. Hildebrandt, B. Friedrich, O. Lenz, P. Scheerer, Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase, Nature Chemical Biology 2014, 10, 378–385.

Y. J. Kim, K. P. Hofmann, O. P. Ernst, P. Scheerer, H. W. Choe, M. E. Sommer, Crystal structure of pre-activated arrestin p44, Nature 2013, 497, 142–146.

H.-W. Choe, Y. J. Kim, J. H. Park, T. Morizumi, E. F. Pai, N. Krauss, K. P. Hofmann, P. Scheerer, O. P. Ernst, Crystal structure of metarhodopsin II, Nature 2011, 471, 651–55.

J. Fritsch, P. Scheerer, S. Frielingsdorf, S. Kroschinsky, B. Friedrich, O. Lenz, C. M. Spahn, The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre, Nature 2011, 479, 249–252.

J. H. Park, P. Scheerer, K. P. Hofmann, H. W. Choe, O. P. Ernst, Crystal structure of the ligand-free G-protein-coupled receptor opsin, Nature 2008, 454, 183–187.

P. Scheerer, J. H. Park, P. W. Hildebrand, Y. J. Kim, N. Krauss, H. W. Choe, K. P. Hofmann, O. P. Ernst, Crystal structure of opsin in its G-protein-interacting conformation, Nature 2008, 455, 497–502.