More information on the web page of our laboratory.
Afiliation: Institute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-252 50 Vestec, Prague West, Czech Republic
Researcher ID: G-3573-2014
ORCID: 0000-0002-8083-7980
Research Interests:
Protein structure and structure-function analysis
Single crystal X-ray diffraction
Structure phasing techniques
Enzymatic catalysis
Non-specific nucleases
Natural killer cell receptors
Bacterial transcription
Infrastructures for structural biology research
Teaching biological crystallography and diffraction techniques
Selected papers
Skalova T, Blaha J, Harlos K, Duskova J, Koval’ T, Stransky J, Hasek J, Vanek O, Dohnalek J. Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states. Acta Crystallographica Section D-Biological Crystallography. 2015;71:578-91. PMC4356368
Dohnalek J, McAuley KE, Brzozowski AM, Østergaard PR, Svendsen A, Wilson KS. Stabilization of Enzymes by Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family. Chapter in Understanding enzymes; Function, Design, Engineering and Analysis, Pan Stanford Publishing, ed. A. Svendsen, 2016, 203-266, ISBN 789814669320, DOI: 10.4032/9789814669337. Available here.
Stranava M, Man P, Skálová T, Kolenko P, Blaha J, Fojtikova V, Martínek V, Dohnálek J, Lengalova A, Rosůlek M, Shimizu T, Martínková M. Coordination and redox state-dependent structural changes of the heme-based oxygen sensor AfGcHK associated with intraprotein signal transduction. J Biol Chem. 2017 Dec 22;292(51):20921-20935. doi: 10.1074/jbc.M117.817023.
Koval T, Dohnalek J. Characteristics and application of S1-P1 nucleases in biotechnology and medicine. Biotechnol. Adv. Epub 2017 Dec 14, 10.1016/j.biotechadv.2017.12.007.
Kovaľová T., Kovaľ T., Benešová E., Vodičková P., Spiwok V., Lipovová P., Dohnálek J. Active site complementation and hexameric arrangement in the GH family 29; a structure-function study of α-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus. Glycobiology 2019; 29: 59-73. https://doi.org/10.1093/glycob/cwy078.
Trundová M, Kovaľ T, Owens RJ, Fejfarová K, Dušková J, Kolenko P, Dohnálek J. Highly stable single-strand-specific 3′-nuclease/nucleotidase from Legionella pneumophila. Int J Biol Macromol, Epub Mar 23 2018, pii: S0141-8130(18)30276-9. doi: 10.1016/j.ijbiomac.2018.03.113.
Kovaľ T, Sudzinová P, Perháčová T, Trundová M, Skálová T, Fejfarová K, Šanderová H, Krásný L, Dušková J, Dohnálek J. Domain structure of HelD, an interaction partner of Bacillus subtilis RNA polymerase. FEBS Lett. 2019 May;593(9):996-1005. doi: 10.1002/1873-3468.13385.
Kovaľ T, Švecová L, Østergaard LH, Skalova T, Dušková J, Hašek J, Kolenko P, Fejfarová K, Stránský J, Trundová M, Dohnálek J. Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer. Sci Rep. 2019 Sep 23;9(1):13700. doi: 10.1038/s41598-019-50105-3.
Structures in PDB: total 62, last five years 27:
5FAX, 5FB9, 5FBA, 5FBB, 5FBC, 5FBD, 5FBF, 5FBG, 5FBZ, 5FFN, 5FJI, 5EH1, 5FJJ, 5J2S, 5MGR, 5MGS, 5MGT, 5OHE, 5OHF, 6EJS, 6EJT, 6EJU, 6EJV, 6GN6, 6I3J, 6I3K, 6I3L.