Prof. Dr. Tilman Schirmer

University of Basel
Klingelbergstrasse 50 / 70
CH - 4056 Basel
Biozentrum, Room 311 Phone: +41 61 267 20 89
Curriculum Vitae

Administrative Assistant

Alexandra Eberhardt
Biozentrum, Room 308
Phone: +41 61 267 20 81


Bacterial second messenger switches enzyme into “reverse gear”

The signaling molecule c-di-GMP plays a crucial role in bacterial reproduction....more

The clock is ticking: Self-activating protein stops growth of bacteria

During periods of nutrient deprivation or stress bacteria stop their growth. A...more

Heading towards a new spin-off at the Biozentrum

The Commission for Technology and Innovation (CTI) is funding the project...more

Research group Tilman Schirmer

How do proteins communicate at the molecular level?

High-resolution structures reveal the mechanisms of signal transduction via the bacterial second messenger c-di-GMP and how the FIC domain can catalyze AMP transfer onto target proteins in a controlled way.

Active center of a Fic enzyme with bound ATP substrate.

Proteins are a major component of cells and fulfill many different functions. We are using X-ray crystallography to determine their three-dimensional structures at the atomic level to deduce their mechanism of action.

How second messengers activate bacteria

Cyclic di-GMP, a small molecule composed of two nucleotides, acts as a transmitter in the bacterial cell. The concentration of the transmitter in the bacterial cell regulates bacterial life-style, in particular the transition from a sessility to mobility. Our research focuses on the enzymes responsible for the synthesis and breakdown of this transmitter, and on the down-stream c-di-GMP receptors. The spatial structures show how the activity of these enzymes is controlled by extrinsic signals, thus regulating the concentration of the transmitter in the cell. Elucidation of the molecular mechanism of this signaling pathway opens new ways for the development of drugs against bacterial pathogens.

How bacterial proteins disrupt signaling pathways in the host cells

Certain bacteria inject proteins into the host cell in order to alter cell function to their advantage. We are working on a newly discovered class of these so-called effector proteins that disable specific host proteins in a targeted manner by attachment of the small molecule AMP. Interestingly, the bacteria protect themselves from the action of these toxic proteins by producing an antitoxin. Structures show how this works and give new ideas how one could inactivate effector proteins within the host cell.