- Protein Classification
- Protein Links
 | out side |
| in side |
| 1qjp » Outer membrane protein A (OMPA), disordered loops | |
|---|---|
| Hydrophobic Thickness | 25.4 ± 1.5 Å |
| Tilt Angle | 11 ± 1° |
| ΔGtransfer | -29.5 kcal/mol |
| Links to 1qjp | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | subunit A (N-terminus in) |
| Resolution | 1.65 Å |
| Other PDB entries of this protein | 1bxw, 1g90, 2ge4, 2jmm, 3nb3 |
| Number of TM Secondary Structures | 8 |
| 1 transmembrane subunit |
|---|
| A - Tilt: 2° - Segments: 1(7-15), 2(35-45), 3(49-58), 4(76-85), 5(91-101), 6(120-131), 7(135-144), 8(160-169) |
| Experimental Verification for 1qjp » Outer membrane protein A (OMPA), disordered loops |
|---|
| Four interfacial Trp residues of OmpA are located at distances of 8-13 Å from the calculated bilayer center. This is close to 9-10 Å obtained by the parallax method (Kleinschmidt and Tamm 1999). Average tilt angle of TM beta-strands (39°) is slightly smaller than estimated by ATR FTIR (46°)(Ramakrishnan et al. 2005). |
| 2 references |
|---|
| Kleinschmidt JH, and Tamm LK (1999) Time-resolved distance determination by tryptophan fluorescence quenching: Probing intermediates in membrane protein folding. Biochemistry38: 4996-5005. PubMed |
| Ramakrishnan M, Qu J, Pocanschi CL, Kleinschmidt JH, and Marsh D (2005) Orientation of beta-barrel proteins OmpA and FhuA in lipid membranes. Chain length dependence from infrared dichroism. Biochemistry 44: 3515-3523. PubMed |
| Comments on 1qjp » Outer membrane protein A (OMPA), disordered loops |
|---|
| OmpA is required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. It also serves as a receptor for a number of T-even like phages and can act as a porin with low permeability that allows slow penetration of small solutes. |
