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.

Czech national centre of European Research Infrastructure Consortium INSTRUCT ERIC.

Day of National Research Infrastructures 2017

Events

  • Monday – Thursday

    23 Oct – 26 Oct

    Biomacromolecular Crystallization Workshop

    Second 4-day crystallization workshop will be focused on Biomacromolecular crystallization techniques.

  • Tuesday – Wednesday

    24 Oct – 25 Oct

    Talking Colors: Advanced Microscopy

    Study of functions and structures of human protein complexes and essential interactions of biomolecules in live cells.

  • Approximately

    October

    MALDI-MS profiling course

    Training in utilization of MALDI-MS profiling method for bacteria identification (focused on master and PhD students).

Event calendar

Research highlights

A model of RNA polymerase II bound to the transcription termination factor Rtt103. The structural model was created using integrative structural biology.

Richard Štefl Research group

Significance

RNA polymerase II (RNAPII) not only transcribes protein coding genes and many noncoding RNA, but also coordinates transcription and RNA processing. This coordination is mediated by a long C-terminal domain (CTD) of the largest RNAPII subunit, which serves as a binding platform for many RNA/protein-binding factors involved in transcription regulation. In this work, we used a hybrid approach to visualize the architecture of the full-length CTD in complex with the transcription termination factor Rtt103. Specifically, we first solved the structures of the isolated subcomplexes at high resolution and then arranged them into the overall envelopes determined at low resolution by small-angle X-ray scattering. The reconstructed overall architecture of the Rtt103–CTD complex reveals how Rtt103 decorates the CTD platform.

 

Jasnovidova, O.; Klumpler, T.; Kubicek, K.; Kalynych, S.; Plevka, P.; Stefl, R. PNAS, Structure and dynamics of the RNAPII CTDsome with Rtt103 PNAS, published ahead of print October 4, 2017, doi:10.1073/pnas.1712450114

 

High-resolution structure of a stable G-hairpin calculated from NMR data (PDB ID: 5M1W). (A) Ten lowest-energy structures. Loop residues are colored orange and O4′ atoms are colored red. (B) Schematic representation of hairpin folding topology. Chain reversal arrangement of the backbone and the 3′-to-5′ stacking of the terminal residues are indicated by dark green and magenta arrows, respectively. Anti and syn guanines that form G:G base pairs are colored dark and light blue, respectively.

Lukáš Trantírek Research Group

Significance 

The first atomic resolution structure of a stable G-hairpin formed by a natively occurring DNA sequence is reported. An 11-nt long G-rich DNA oligonucleotide, 5′-d(GTGTGGGTGTG)-3′, corresponding to the most abundant sequence motif in irregular telomeric DNA from Saccharomyces cerevisiae adopts a novel type of mixed parallel/antiparallel fold-back DNA structure, which is stabilized by dynamic G:G base pairs that transit between N1-carbonyl symmetric and N1-carbonyl, N7-amino base-pairing arrangements. The structure reveals previously unknown principles of the folding of G-rich oligonucleotides that could be applied to the prediction of natural and/or the design of artificial recognition DNA elements. The structure also demonstrates that the folding landscapes of short DNA single strands is much more complex than previously assumed.

Gajarsky, M.;  Zivkovic, M. L. ;  Stadlbauer, P. ; Pagano, B.;  Fiala, R.;  Amato, J.;  Tomaska, L.;  Sponer, J.;  Plavec, J.;  Trantirek, L., Structure of a Stable G-Hairpin JACS 139, 3591-3594, doi:10.1021/jacs.6b10786 (2017)

 

More publications Research Highlights archive

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