2MHL
NMR solution Structure of the E.coli Outer Membrane Protein W
Summary for 2MHL
| Entry DOI | 10.2210/pdb2mhl/pdb |
| NMR Information | BMRB: 19637 |
| Descriptor | Outer membrane protein W (1 entity in total) |
| Functional Keywords | integral membrane protein, beta barrel, outer membrane protein, membrane protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 21002.42 |
| Authors | Horst, R.,Stanczak, P.,Wuthrich, K. (deposition date: 2013-11-26, release date: 2014-08-06, Last modification date: 2024-05-15) |
| Primary citation | Horst, R.,Stanczak, P.,Wuthrich, K. NMR Polypeptide Backbone Conformation of the E. coli Outer Membrane Protein W. Structure, 22:1204-1209, 2014 Cited by PubMed Abstract: The outer membrane proteins (Omps) are key factors for bacterial survival and virulence. Among the Omps that have been structurally characterized either by X-ray crystallography or by NMR in solution, the crystal structure of OmpW stands out because three of its four extracellular loops are well defined, whereas long extracellular loops in other E. coli Omps are disordered in the crystals as well as in NMR structures. OmpW thus presented an opportunity for a detailed comparison of the extracellular loops in a β-barrel membrane protein structure in crystals and in noncrystalline milieus. Here, the polypeptide backbone conformation of OmpW in 30-Fos micelles was determined. Complete backbone NMR assignments were obtained and the loops were structurally characterized. In combination with the OmpW crystal structure, NMR line shape analyses, and (15)N{(1)H}-NOE data, these results showed that intact regular secondary structures in the loops undergo slow hinge motions at the detergent-solvent interface. PubMed: 25017731DOI: 10.1016/j.str.2014.05.016 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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