1G90
NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers
Summary for 1G90
| Entry DOI | 10.2210/pdb1g90/pdb |
| Related | 1QJP |
| Descriptor | OUTER MEMBRANE PROTEIN A (1 entity in total) |
| Functional Keywords | beta barrel, integral membrane protein, membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P0A910 |
| Total number of polymer chains | 1 |
| Total formula weight | 19060.98 |
| Authors | Arora, A.,Abildgaard, F.,Bushweller, J.H.,Tamm, L.K. (deposition date: 2000-11-21, release date: 2001-04-21, Last modification date: 2024-05-22) |
| Primary citation | Arora, A.,Abildgaard, F.,Bushweller, J.H.,Tamm, L.K. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy Nat.Struct.Biol., 8:334-338, 2001 Cited by PubMed Abstract: We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of an eight-stranded beta-barrel connected by tight turns on the periplasmic side and larger mobile loops on the extracellular side. The solution structure of the barrel in DPC micelles is similar to that in n-octyltetraoxyethylene (C(8)E(4)) micelles determined by X-ray diffraction. Moreover, data from NMR dynamic experiments reveal a gradient of conformational flexibility in the structure that may contribute to the membrane channel function of this protein. PubMed: 11276254DOI: 10.1038/86214 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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