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Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance

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Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR.

Mohammed Kaplan¹, Abhishek Cukkemane¹, Gydo C P van Zundert¹

¹NMR Spectroscopy, Utrecht University, Utrecht, the Netherlands.

|May 19, 2015

Summary

Researchers used advanced solid-state nuclear magnetic resonance to study the bacterial type IV secretion system core complex (T4SScc) in its native cellular environment. This confirmed the complex

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Area of Science:

Structural biology
Microbiology
Biophysics

Background:

The bacterial type IV secretion system core complex (T4SScc) is crucial for protein transport.
Understanding T4SScc structure in situ is vital for elucidating its function.

Purpose of the Study:

To validate a previously proposed structural model of T4SScc.
To investigate the T4SScc structure within its native cellular environment at atomic resolution.

Main Methods:

Cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance (dNP-ssNMR) spectroscopy was employed.
Integration of in vitro and in silico data was used to generate an initial structural model.

Main Results:

The T4SScc was confirmed to be well-folded within the bacterial cellular setting.
Previously uncharacterized protein regions of the T4SScc were identified in situ.

Conclusions:

The study validates the structural model of T4SScc in a native cellular context.
Cellular dNP-ssNMR provides atomic-resolution insights into complex biomolecular structures within cells.