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14–17 Mar 2022
Europe/Berlin timezone

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

14 Mar 2022, 14:50
20m
Talk Biologic Structure, Function, Reactivity, and Regulation Biocrystallography: Enzymes

Speaker

Wulf Blankenfeldt (DGK)

Description

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 ligand-mediated oligomerization may hence establish a self-protection mechanism.

Primary authors

Prof. Antje Flieger (Robert Koch Institute, Wernigerode) Dr Maurice Diwo (Helmholtz Centre for Infection Research) Wulf Blankenfeldt (DGK) Dr Wiebke Michel (Robert Koch Institute, Wernigerode)

Presentation materials