Viral and Microbial Proteins | Iva Pichová Group

About our group

The research of our laboratory focuses mainly on functional and structural studies of key proteins from Hepatitis B virus and Mycobacteria spp and their interactions with cellular proteins. We also study proteins from pathogenic yeasts and cooperate with chemical ecologists on insect pheromone biosynthetic enzymes.

Research projects involve protein engineering, protein purification, protein characterization, enzymology, NMR and X-ray protein structure solution, isolation and analysis of complexes of cellular and pathogenic proteins, various molecular biological methods, and electron microscopy analysis. Our close cooperation with organic chemists facilitates multidisciplinary research focused on identification and characterization of enzymes involved in drug metabolism and testing of potential inhibitors.

The group is a member of the Gilead Sciences & IOCB Research Centre, NPU 1 and OPVVV projects.

News

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2 December 2019

New Ph.D. students

28 November 2019

Dája placed third in high school student competition

Understanding desaturation/hydroxylation activity of castor stearoyl Δ<sup>9</sup>-Desaturase through rational mutagenesis

Understanding desaturation/hydroxylation activity of castor stearoyl Δ⁹-Desaturase through rational mutagenesis

M. Tupec M. Culka A. Machara S. Macháček D. Bím A. Svatoš L. Rulíšek I. Pichová

Computational and Structural Biotechnology Journal 20: 1378-1388 (2022)

A recently proposed reaction mechanism of soluble Δ⁹ desaturase (Δ⁹D) allowed us to identify auxiliary residues His203, Asp101, Thr206 and Cys222 localized near the di-iron active site that are supposedly involved in the proton transfer (PT) to and from the active site. The PT, along with the electron transfer (ET), seems to be crucial for efficient desaturation. Thus, perturbing the major PT chains is expected to impair the native reaction and (potentially) amplify minor reaction channels, such as the substrate hydroxylation. To verify this hypothesis, we mutated the four residues mentioned above into their counterparts present in a soluble methane monooxygenase (sMMO), and determined the reaction products of mutants. We found that the mutations significantly promote residual monohydroxylation activities on stearoyl-CoA, often at the expense of native desaturation activity. The favored hydroxylation positions are C₉, followed by C₁₀ and C₁₁. Reactions with unsaturated substrate,…

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Biogenesis of hepatitis B virus e antigen is driven by translocon-associated protein complex and regulated by conserved cysteine residues within its signal peptide sequence

H. Zábranská A. Zábranský B. Lubyová J. Hodek A. Křenková M. Hubálek J. Weber I. Pichová

FEBS Journal 2022: Early View

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Structural determinants for subnanomolar inhibition of the secreted aspartic protease Sapp1p from Candida parapsilosis

J. Dostál J. Brynda L. Vaňková S. R. Zia O. Heidingsfeld M. Lepšík

Journal of Enzyme Inhibition and Medicinal Chemistry 36 (1): 914-921 (2021)

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Phosphofructokinases A and B from Mycobacterium tuberculosis Display Different Catalytic Properties and Allosteric Regulation

J. Snášel I. Machová V. Šolínová V. Kašička M. Krečmerová I. Pichová

International Journal of Molecular Sciences 22 (3): 1483 (2021)

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