2F1V
Outer membrane protein OmpW
Summary for 2F1V
| Entry DOI | 10.2210/pdb2f1v/pdb |
| Related | 2F1T |
| Descriptor | Outer membrane protein W, GLYCEROL (2 entities in total) |
| Functional Keywords | outer membrane protein beta barrel, membrane protein |
| Biological source | Escherichia coli K12 |
| Cellular location | Cell outer membrane: P0A915 |
| Total number of polymer chains | 6 |
| Total formula weight | 130753.18 |
| Authors | van den Berg, B. (deposition date: 2005-11-15, release date: 2006-01-24, Last modification date: 2023-08-23) |
| Primary citation | Hong, H.,Patel, D.R.,Tamm, L.K.,van den Berg, B. The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel. J.Biol.Chem., 281:7568-7577, 2006 Cited by PubMed Abstract: Escherichia coli OmpW belongs to a family of small outer membrane proteins that are widespread in Gram-negative bacteria. Their functions are unknown, but recent data suggest that they may be involved in the protection of bacteria against various forms of environmental stress. To gain insight into the function of these proteins A we have determined the crystal structure of E. coli OmpW to 2.7-A resolution. The structure shows that OmpW forms an 8-stranded beta-barrel with a long and narrow hydrophobic channel that contains a bound n-dodecyl-N,N-dimethylamine-N-oxide detergent molecule. Single channel conductance experiments show that OmpW functions as an ion channel in planar lipid bilayers. The channel activity can be blocked by the addition of n-dodecyl-N,N-dimethylamine-N-oxide. Taken together, the data suggest that members of the OmpW family could be involved in the transport of small hydrophobic molecules across the bacterial outer membrane. PubMed: 16414958DOI: 10.1074/jbc.M512365200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
