1QJP
HIGH RESOLUTION STRUCTURE OF THE OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN
Summary for 1QJP
| Entry DOI | 10.2210/pdb1qjp/pdb |
| Related | 1BXW |
| Descriptor | OUTER MEMBRANE PROTEIN A, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total) |
| Functional Keywords | outer membrane |
| Biological source | ESCHERICHIA COLI BL21(DE3) |
| Total number of polymer chains | 1 |
| Total formula weight | 20634.35 |
| Authors | Pautsch, A.,Schulz, G.E. (deposition date: 1999-06-29, release date: 2000-06-30, Last modification date: 2023-12-13) |
| Primary citation | Pautsch, A.,Schulz, G.E. High Resolution Structure of the Ompa Membrane Domain J.Mol.Biol., 298:273-, 2000 Cited by PubMed Abstract: The membrane domain of OmpA consists of an eight-stranded all-next-neighbor antiparallel beta-barrel with short turns at the periplasmic barrel end and long flexible loops at the external end. The structure analysis has been extended from medium resolution to 1. 65 A (1 A=0.1 nm), and the molecular model has been refined anisotropically to show oriented mobilities of the structural elements. The improved data allowed us to locate five further detergent molecules and 11 more water molecules. Moreover, the two large non-polar packing contacts have now been defined in detail. The analysis indicates that the beta-barrel constitutes a solid scaffold such that the long external loops need not contribute to stability. These loops are highly mobile and thus cause a major problem during the crystallization process. The beta-barrel was related to those of lipocalins. Two further crystal forms with exceptionally dense packing arrangements were established at medium resolution. PubMed: 10764596DOI: 10.1006/JMBI.2000.3671 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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