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NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.

Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, Choe S
Science 307 1317-21 (2005)
Cited: 146 times
EuropePMC logo PMID: 15731457

Abstract

Although structure determination of soluble proteins has become routine, our understanding of membrane proteins has been limited by experimental bottlenecks in obtaining both sufficient yields of protein and ordered crystals. Mistic is an unusual Bacillus subtilis integral membrane protein that folds autonomously into the membrane, bypassing the cellular translocon machinery. Using paramagnetic probes, we determined by nuclear magnetic resonance (NMR) spectroscopy that the protein forms a helical bundle with a surprisingly polar lipid-facing surface. Additional experiments suggest that Mistic can be used for high-level production of other membrane proteins in their native conformations, including many eukaryotic proteins that have previously been intractable to bacterial expression.

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  1. Helical membrane protein conformations and their environment. Cross TA, Murray DT, Watts A. Eur Biophys J 42 731-755 (2013)
  2. Engineered Chimera Protein Constructs to Facilitate the Production of Heterologous Transmembrane Proteins in E. coli. Ogunbowale A, Georgieva ER. Int J Mol Sci 25 2354 (2024)

Articles - 1ygm mentioned but not cited (7)

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