2H3O
Structure of MERFT, a membrane protein with two trans-membrane helices
Summary for 2H3O
| Entry DOI | 10.2210/pdb2h3o/pdb |
| Related | 1WAZ |
| Descriptor | MerF (1 entity in total) |
| Functional Keywords | membrane protein, alpha-helix, bicelle |
| Biological source | Morganella morganii |
| Total number of polymer chains | 1 |
| Total formula weight | 6408.63 |
| Authors | Opella, S.J.,De Angelis, A.A.,Howell, S.C.,Nevzorov, A.A. (deposition date: 2006-05-22, release date: 2006-10-03, Last modification date: 2024-05-29) |
| Primary citation | De Angelis, A.A.,Howell, S.C.,Nevzorov, A.A.,Opella, S.J. Structure Determination of a Membrane Protein with Two Trans-membrane Helices in Aligned Phospholipid Bicelles by Solid-State NMR Spectroscopy. J.Am.Chem.Soc., 128:12256-12267, 2006 Cited by PubMed Abstract: The structure of the membrane protein MerFt was determined in magnetically aligned phospholipid bicelles by solid-state NMR spectroscopy. With two trans-membrane helices and a 10-residue inter-helical loop, this truncated construct of the mercury transport membrane protein MerF has sufficient structural complexity to demonstrate the feasibility of determining the structures of polytopic membrane proteins in their native phospholipid bilayer environment under physiological conditions. PISEMA, SAMMY, and other double-resonance experiments were applied to uniformly and selectively (15)N-labeled samples to resolve and assign the backbone amide resonances and to measure the associated (15)N chemical shift and (1)H-(15)N heteronuclear dipolar coupling frequencies as orientation constraints for structure calculations. (1)H/(13)C/(15)N triple-resonance experiments were applied to selectively (13)C'- and (15)N-labeled samples to complete the resonance assignments, especially for residues in the nonhelical regions of the protein. A single resonance is observed for each labeled site in one- and two-dimensional spectra. Therefore, each residue has a unique conformation, and all protein molecules in the sample have the same three-dimensional structure and are oriented identically in planar phospholipid bilayers. Combined with the absence of significant intensity near the isotropic resonance frequency, this demonstrates that the entire protein, including the loop and terminal regions, has a well-defined, stable structure in phospholipid bilayers. PubMed: 16967977DOI: 10.1021/ja063640w PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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