Regensburg 2013 – scientific programme
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BP: Fachverband Biologische Physik
BP 8: Posters: Proteins
BP 8.9: Poster
Monday, March 11, 2013, 17:30–19:30, Poster B2
Investigation of enzyme complex dynamics via atomic force microscopy — •Mitja Platen1, Sabin Prajapati2, Kathrin Schröder-Tittmann2, Kai Tittmann2, and Iwan Schaap1 — 1III. Physikalisches Institut, Georg August Universität Göttingen, Germany — 2Albrecht-von-Haller-Institut, Georg August Universität Göttingen, Germany
The pyruvate dehydrogenase multienzyme complex (PDHc) links glycolysis to the citric acid cycle by converting central metabolite pyruvate into acetyl-CoA, a building block for many fundamental metabolic pathways. The core of the human PDHc consists of 60 dihydrolipoamide acetyltransferase enzymes (E2), which assemble into a 50 nm diameter dodecahedral structure. A key trait vital to PDHc function is the flexibility of the N-terminal "swinging lipoyl domain" of E2, which is capable of reaching the active sites of all proximal enzyme components. Although low resolution structural information about the PDHc is available, the underlying dynamics of catalysis, in particular substrate channeling, is not understood.
To be able to observe the structure of single PDH complexes we are applying AFM in liquid. Ultimately, we aim to observe the core dynamics at real-time via optimization of imaging techniques by exploring the limits of amplitude and frequency modulation as well as jumping mode AFM. We will present our approach to maximize the spatial and temporal resolution and will present our first results on this enzyme complex.