Yiseul Shin

Area of research

Infectious Diseases · Electronic, Optical and Magnetic Materials

Research interest

Research topics from publications: Mycobacterium tuberculosis CrgA Forms a Dimeric Structure with Its Transmembrane Domain Sandwiched between Cytoplasmic and Periplasmic β-Sheets, Enabling Multiple Interactions with Other Divisome Proteins; Unique Insights into the Structural and Functional Biology of Membrane Proteins from Solid State NMR Spectroscopy; Structural Characterization of the Full Length CrgA Protein Found in Mycobacterium Tuberculosis; Understanding the Role of the N-Terminal CrgA Interactions with FtsZ in the Mycobacterium Tuberculosis Divisome; Structural Characterization of the N-Terminus of CRGA: An Intrinsically Disordered Region and Short β Strands to Stabilize Dimerization; Characterization of the Extra-Membrane Domains of CrgA in Lipid Bilayers using Solid State NMR. Representative work: CrgA is a key transmembrane (TM) protein in the cell division process of Mycobacterium tuberculosis (Mtb), the pathogen responsible for tuberculosis. While many of the Mtb divisome proteins have been identified, their structures and interactions remain largely unknown. Previous studies of CrgA using oriented-sample solid-state NMR have defined the tilt and rotation of the TM helices, but the cytoplasmic and periplasmic domains and even the oligomeric state were uncharacterized. Here, by combining oriented-sample and magic-angle spinning solid-state NMR spectra, we solved the full-length structure of CrgA. The structure features a dimer with a TM domain sandwiched between a cytoplasmic β-shee

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