Czech Infrastructure for Integrative Structural Biology – CIISB
A gateway to realm of structural data for biochemists, biophysicists, molecular biologist, and all scientists whose research benefits from accurate structure determination of biological macromolecules, assemblies, and complex molecular machineries at atomic resolution.
Open access to 10 high-end core facilities and assisted expertise in NMR, X-ray crystallography and crystallization, cryo-electron microscopy and tomography, biophysical characterization of biomolecular interaction, nanobiotechnology, proteomics and structural mass spectrometry.
A distributed infrastructure constituted by Core Facilities of CEITEC (Central European Institute of Technology), located in Brno, and BIOCEV (Biotechnology and Biomedicine Centre), located in Vestec near Prague, Central Bohemia.
CEITEC Core Facilities
BIOCEV Core Facilities
Velké výzkumné infrastruktury - Operated by CESNET on behalf of the Council for Large Infrastructures for Research, Experimental Development and Innovation.
Automatic sample changer and optic upgrade at the X-ray Diffraction and Bio-SAXS core facility at CEITEC MU
The automatic sample changer for BioSAXS Kratky camera system was installed and it is in operation.
POSTDOC: PROTEIN STRUCTURAL BIOLOGIST
We are seeking for a highly motivated scientist for EU-funded postdoctoral position inprotein structural biology for experimental team at Loschmidt Laboratories, Masaryk University, Brno, Czech Republic.
4th National Day of Large Research Infrastructures
The Ministry of Education, Youth and Sports of the Czech Republic and the Faculty of Mathematics and Physics of Charles University are honoured to invite you to take part in the 4th National Day of Large Research Infrastructures, to be held on 19th November 2019 in the premises of LINDAT/CLARIAH-CZlarge research infrastructure.
NAT. COMMUN. 2019
Summary showing CK1ε role in DVL3 conformational dynamics. A summarizing model which proposes at least three DVL conformations in vivo: (i) a closed (CK1ε present and inactive), (ii) open (CK1ε active), and (iii) non-physiological open, which occurs when CK1ε is absent or the DVL-CK1ε interaction is disrupted. Position of insertion of FlAsH III binding tag is indicated. The CK1-induced phosphorylation events are depicted as P in red circle and the C-terminus of DVL as red thick line. The molecular distance analysed in the FRET FlAsH sensor III is shown as a dashed red line; ECFP, enhanced cyan fluorescent protein
Dishevelled (DVL) is the key component of the Wnt signalling pathway. Currently, DVL conformational dynamics under native conditions is unknown. To overcome this limitation, we develop the Fluorescein Arsenical Hairpin Binder- (FlAsH-) based FRET in vivo approach to study DVL conformation in living cells. Using this single-cell FRET approach, we demonstrate that (i) Wnt ligands induce open DVL conformation, (ii) DVL variants that are predominantly open, show more even subcellular localization and more efficient membrane recruitment by Frizzled (FZD) and (iii) Casein kinase 1 ɛ (CK1ɛ) has a key regulatory function in DVL conformational dynamics. In silico modelling and in vitro biophysical methods explain how CK1ɛ-specific phosphorylation events control DVL conformations via modulation of the PDZ domain and its interaction with DVL C-terminus. In summary, our study describes an experimental tool for DVL conformational sampling in living cells and elucidates the essential regulatory role of CK1ɛ in DVL conformational dynamics.
Harnoš, J., Cañizal, M.C.A., Jurásek, M., Kumar, J., Holler, C., Schambony, A., Hanáková, K., Bernatík, O., Zdráhal, Z. Gömöryová, K.,Gybel’,T., Radaszkiewicz, T.W., Kravec, M., Trantírek, L., Ryneš, J., Dave, Z., Fernández-Llamazares, A.I., Vácha, R., Tripsianes, K., Hoffmann, C., and Bryja, V.: Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1, Nat. Commun. (2019) 10, 1804, 1-18. doi.org/10.1038/s41467-019-09651-7
NAT. COMMUN. 2019
Scheme of enterovirus genome release. Binding to receptors or exposure to acidic pH in endosomes induces conformational transition of virions to activated particles. The structural changes within the capsid and virus RNA enable the expulsion of pentamers from the capsid, resulting in the formation of open particles. The RNA genomes are released from the open particles. After the genome release, the pentamers may re-associate with the open capsids. Scale bar represents 10 nm
Viruses from the genus Enterovirusare important human pathogens. Receptor binding or exposure to acidic pH in endosomes converts enterovirus particles to an activated state that is required for genome release. However, the mechanism of enterovirus uncoating is not well understood. Here, we use cryo-electron microscopy to visualize virions of human echovirus 18 in the process of genome release. We discover that the exit of the RNA from the particle of echovirus 18 results in a loss of one, two, or three adjacent capsid-protein pentamers. The opening in the capsid, which is more than 120 Å in diameter, enables the release of the genome without the need to unwind its putative double-stranded RNA segments. We also detect capsids lacking pentamers during genome release from echovirus 30. Thus, our findings uncover a mechanism of enterovirus genome release that could become target for antiviral drugs
Buchta, D., Füzik, T., Hrebík, D., Levdansky, Y., Sukeník, L., Mukhamedova, L., Moravcová, J., Vácha, R., and Plevka, P: Enterovirus particles expel capsid pentamers to enable genome release, Nat. Commun. (2019)10, 1138, 1-9 doi.org/10.1038/s41467-019-09132-x