1ORM
NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES
Summary for 1ORM
| Entry DOI | 10.2210/pdb1orm/pdb |
| Related | 1QJ8 1QJ9 |
| Descriptor | Outer membrane protein X (1 entity in total) |
| Functional Keywords | ompx, membrane protein, trosy, dhpc, detergents, lipids, micelles |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P0A917 |
| Total number of polymer chains | 1 |
| Total formula weight | 16371.77 |
| Authors | Fernandez, C.,Adeishvili, K.,Wuthrich, K. (deposition date: 2003-03-14, release date: 2003-04-22, Last modification date: 2024-05-22) |
| Primary citation | FERNANDEZ, C.,ADEISHVILI, K.,WUTHRICH, K. TRANSVERSE RELAXATION-OPTIMIZED NMR SPECTROSCOPY WITH THE OUTER MEMBRANE PROTEIN OMPX IN DIHEXANOYL PHOSPHATIDYLCHOLINE MICELLES Proc.Natl.Acad.Sci.USA, 98:2358-2363, 2001 Cited by PubMed Abstract: The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX from Escherichia coli was reconstituted with dihexanoyl phosphatidylcholine (DHPC) in mixed micelles of molecular mass of about 60 kDa. Transverse relaxation-optimized spectroscopy (TROSY)-type triple resonance NMR experiments and TROSY-type nuclear Overhauser enhancement spectra were recorded in 2 mM aqueous solutions of these mixed micelles at pH 6.8 and 30 degrees C. Complete sequence-specific NMR assignments for the polypeptide backbone thus have been obtained. The (13)C chemical shifts and the nuclear Overhauser effect data then resulted in the identification of the regular secondary structure elements of OmpX/DHPC in solution and in the collection of an input of conformational constraints for the computation of the global fold of the protein. The same type of polypeptide backbone fold is observed in the presently determined solution structure and the previously reported crystal structure of OmpX determined in the presence of the detergent n-octyltetraoxyethylene. Further structure refinement will have to rely on the additional resonance assignment of partially or fully protonated amino acid side chains, but the present data already demonstrate that relaxation-optimized NMR techniques open novel avenues for studies of structure and function of integral membrane proteins. PubMed: 11226244DOI: 10.1073/pnas.051629298 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
