1YGM
NMR structure of Mistic
Summary for 1YGM
| Entry DOI | 10.2210/pdb1ygm/pdb |
| Descriptor | hypothetical protein BSU31320 (1 entity in total) |
| Functional Keywords | alpha-helical bundle, integral membrane protein, membrane protein |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 |
| Total number of polymer chains | 1 |
| Total formula weight | 13653.43 |
| Authors | Roosild, T.P.,Greenwald, J.,Vega, M.,Castronovo, S.,Riek, R.,Choe, S. (deposition date: 2005-01-05, release date: 2005-03-01, Last modification date: 2024-05-22) |
| Primary citation | Roosild, T.P.,Greenwald, J.,Vega, M.,Castronovo, S.,Riek, R.,Choe, S. NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science, 307:1317-1321, 2005 Cited by PubMed 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. PubMed: 15731457DOI: 10.1126/science.1106392 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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