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)

Research Units in UniSysCat

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

UniSysCat Publications

  • Cryo-EM captures early ribosome assembly in action, B. Qin, S. M. Lauer, A. Balke, C. H. Vieira-Vieira, J. Bürger, T. Mielke, M. Selbach, P. Scheerer, C. M. T. Spahn, R. Nikolay, Nature Communications 2023, 14, 1–10, 10.1038/s41467-023-36607-9
  • Structure of the actively translating plant 80S ribosome at 2.2 Å resolution, J. Smirnova, J. Loerke, G. Kleinau, A. Schmidt, J. Bürger, E. H. Meyer, T. Mielke, P. Scheerer, R. Bock, C. M. T. Spahn, R. Zoschke, Nature Plants 2023, 9, 987–1000, 10.1038/s41477-023-01407-y
  • Time‐resolved fluorescence anisotropy with Atto 488‐labeled phytochrome Agp1 from, A. Elkurdi, G. Guigas, L. Hourani‐Alsharafat, P. Scheerer, G. U. Nienhaus, N. Krauß, T. Lamparter, Photochemistry and Photobiology 2023, 1–12, 10.1111/php.13851
  • Stepwise conversion of the Cys [4Fe-3S] to a Cys [4Fe-4S] cluster and its impact on oxygen tolerance of [NiFe]-hydrogenase, A. Schmidt, J. Kalms, C. Lorent, S. Katz, S. Frielingsdorf, R. M. Evans, J. Fritsch, E. Siebert, C. Teutloff, F. A. Armstrong, I. Zebger, O. Lenz, P. Scheerer, Chemical Science 2023, 10.1039/D3SC03739H
  • Intramolecular activity regulation of adhesion GPCRs in light of recent structural and evolutionary information, G. Kleinau, A. H. Ali, F. Wiechert, M. Szczepek, A. Schmidt, C. M. T. Spahn, I. Liebscher, T. Schöneberg, P. Scheerer, Pharmacological Research 2023, 197, 106971–0, 10.1016/j.phrs.2023.106971
  • Is the Neuropeptide PEN a Ligand of GPR83?, Y. Giesecke, V. Asimi, V. Stulberg, G. Kleinau, P. Scheerer, B. Koksch, C. Grötzinger, International Journal of Molecular Sciences 2023, 24, 15117–0, 10.3390/ijms242015117
  • Ultrafast proton-coupled isomerization in the phototransformation of phytochrome, Y. Yang, T. Stensitzki, L. Sauthof, A. Schmidt, P. Piwowarski, F. Velazquez Escobar, N. Michael, A. D. Nguyen, M. Szczepek, F. N. Brünig, R. R. Netz, M. A. Mroginski, S. Adam, F. Bartl, I. Schapiro, P. Hildebrandt, P. Scheerer, K. Heyne, Nature Chemistry 2022, 14, 823–830, 10.1038/s41557-022-00944-x
  • Expression and Characterization of Relaxin Family Peptide Receptor 1 Variants, D. Speck, G. Kleinau, M. Meininghaus, A. Erbe, A. Einfeldt, M. Szczepek, P. Scheerer, V. Pütter, Frontiers in Pharmacology 2022, 12, 10.3389/fphar.2021.826112
  • A cytosolic disulfide bridge‐supported dimerization is crucial for stability and cellular distribution of Coxsackievirus B3 protein 3A, M. Voss, G. Kleinau, N. Gimber, K. Janek, C. Bredow, F. Thery, F. Impens, J. Schmoranzer, P. Scheerer, P. Kloetzel, A. Beling, The FEBS Journal 2022, 289, 3826–3838, 10.1111/febs.16368
  • Resonance Raman spectroscopic analysis of the iron–sulfur cluster redox chain of the membrane‐bound [NiFe]‐hydrogenase, E. Siebert, A. Schmidt, S. Frielingsdorf, J. Kalms, U. Kuhlmann, O. Lenz, P. Scheerer, I. Zebger, P. Hildebrandt, Journal of Raman Spectroscopy 2021, 10.1002/jrs.6163
  • Local Electric Field Changes during the Photoconversion of the Bathy Phytochrome Agp2, A. Kraskov, J. von Sass, A. D. Nguyen, T. O. Hoang, D. Buhrke, S. Katz, N. Michael, J. Kozuch, I. Zebger, F. Siebert, P. Scheerer, M. A. Mroginski, N. Budisa, P. Hildebrandt, Biochemistry 2021, 60, 2967–2977, 10.1021/acs.biochem.1c00426
  • Structures of active melanocortin-4 receptor–Gs-protein complexes with NDP-α-MSH and setmelanotide, N. A. Heyder, G. Kleinau, D. Speck, A. Schmidt, S. Paisdzior, M. Szczepek, B. Bauer, A. Koch, M. Gallandi, D. Kwiatkowski, J. Bürger, T. Mielke, A. G. Beck-Sickinger, P. W. Hildebrand, C. M. T. Spahn, D. Hilger, M. Schacherl, H. Biebermann, T. Hilal, P. Kühnen, B. K. Kobilka, P. Scheerer, Cell Research 2021, 31, 1176–1189, 10.1038/s41422-021-00569-8
  • Design of a light-gated proton channel based on the crystal structure of 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.