DGK conference 2022

Session

Biocrystallography: Enzymes

MS1

Mar 14, 2022, 2:30 PM

Conveners

Biocrystallography: Enzymes

• Wulf Blankenfeldt (DGK)

215. Structural characterization of reaction intermediates of the copper-dependent formylglycine-generating enzyme

Florian Seebeck

3/14/22, 3:50 PM

Talk

O2 activation is central elementary step in many biological reactions. The formylglycine generating enzyme (FGE) is a mononuclear copper enzyme that appears to follow an unusual strategy for O2 activation. In this presentation I will summarize our past and present efforts to visualize individual states of the enzyme on its path from the resting state to the reactive Michaelis Menten complex and beyond.

217. Structures of a DYW domain shed first light on a unique plant RNA editing regulation principle

Mr Gert Weber (Helmholtz-Zentrum Berlin), Gottfried Palm (Universität Greifswald)

3/14/22, 3:10 PM

Talk

The DYW domain, an enzyme for plant RNA editing: Pentatricopeptide repeat (PPR) proteins with a C-terminal DYW domain are responsible for C to U RNA editing in plants. We show that the DYW domain harbors the cytidine deaminase activity by functional data in vitro and structural similarity to distinctly related known cytidine deaminases. A DYW-specific domain regulates the active site...

81. The crystal structure of phospholipase PlaB from Legionella pneumophila reveals the basis of tetramerization-dependent inactivation by a central metabolite

Wulf Blankenfeldt (DGK)

3/14/22, 2:50 PM

Biologic Structure, Function, Reactivity, and Regulation

Talk

PlaB is a secreted phospholipase of Legionella pneumophila, the causative agent of Legionnaires' Disease. It is an unusual enzyme that looses activity at higher concentrations due to tetramer formation.
Here, we show the crystal structure of PlaB in its inactive tetrameric form. We find that the tetramer is stabilized by NAD(H), a central metabolite only found within the cell. This...

87. The crystal structures of post-reactive states of 2’-5’-oligoadenylate synthetase provide new insights into the mechanism of the innate immune signaling

Mr Pavel Kats (Hannover Medical School)

3/14/22, 3:30 PM

Biologic Structure, Function, Reactivity, and Regulation

Talk

The innate immune sensor 2’-5’-oligoadenylate synthetase (OAS) is among the most promising targets for the development of new antivirals. Here we report the results of kinetic crystallography, mutagenesis, and computational chemistry studies of the OAS1 product release mechanism. These investigations provide new insights into the rate-limiting steps of innate immune signaling, which can help...

214. The structural basis of orotidine-5’-phosphate decarboxylase catalysis: Ground-state destabilisation by electrostatic repulsion is not a driving force

Kai Tittmann

3/14/22, 2:30 PM

Biologic Structure, Function, Reactivity, and Regulation

Talk

I will present crystallographic snapshots of the human enzyme orotidine-5-monophosphate decarboxylase in complex with the genuine substrate, substrate analogs, transition state analogs and product - all at true atomic resolution. These snapshots of catalysis defy the proposed mechanism of ground-state destabilization by revealing that the substrate carboxylate is protonated and forms a...