1BXW
OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN
Summary for 1BXW
| Entry DOI | 10.2210/pdb1bxw/pdb |
| Descriptor | PROTEIN (OUTER MEMBRANE PROTEIN A), (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total) |
| Functional Keywords | outer membrane, transmembrane protein, membrane protein |
| Biological source | Escherichia coli BL21(DE3) |
| Cellular location | Cell outer membrane ; Multi-pass membrane protein : P0A910 |
| Total number of polymer chains | 1 |
| Total formula weight | 19199.34 |
| Authors | Schulz, G.E.,Pautsch, A. (deposition date: 1998-10-03, release date: 1998-10-14, Last modification date: 2024-05-22) |
| Primary citation | Pautsch, A.,Schulz, G.E. Structure of the outer membrane protein A transmembrane domain. Nat.Struct.Biol., 5:1013-1017, 1998 Cited by PubMed Abstract: The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1-171, by X-ray diffraction analysis, to a resolution of 2.5 A. It consists of a regular, extended eight-stranded beta-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane. PubMed: 9808047DOI: 10.1038/2983 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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