2GE4
High-resolution solution structure of outer membrane protein A transmembrane domain
Summary for 2GE4
| Entry DOI | 10.2210/pdb2ge4/pdb |
| Related | 1g90 |
| Descriptor | Outer membrane protein A (1 entity in total) |
| Functional Keywords | membrane protein, beta barrel |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P0A910 |
| Total number of polymer chains | 1 |
| Total formula weight | 19192.18 |
| Authors | Cierpicki, T.,Liang, B.,Tamm, L.K.,Bushweller, J.H. (deposition date: 2006-03-17, release date: 2006-04-11, Last modification date: 2024-05-29) |
| Primary citation | Cierpicki, T.,Liang, B.,Tamm, L.K.,Bushweller, J.H. Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A. J.Am.Chem.Soc., 128:6947-6951, 2006 Cited by PubMed Abstract: The structure determination of membrane proteins is one of the most challenging applications of solution NMR spectroscopy. The paucity of distance information available from the highly deuterated proteins employed requires new approaches in structure determination. Here we demonstrate that significant improvement in the structure accuracy of the membrane protein OmpA can be achieved by refinement with residual dipolar couplings (RDCs). The application of charged polyacrylamide gels allowed us to obtain two alignments and accurately measure numerous heteronuclear dipolar couplings. Furthermore, we have demonstrated that using a large set of RDCs in the refinement can yield a structure with 1 A rms deviation to the backbone of the high-resolution crystal structure. Our simulations with various data sets indicate that dipolar couplings will be critical for obtaining accurate structures of membrane proteins. PubMed: 16719475DOI: 10.1021/ja0608343 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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