PDB ID or protein name

1qjp » Outer membrane protein A (OMPA), disordered loops

1qjp » Outer membrane protein A (OMPA), disordered loops
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Topology in Bacterial Gram-negative outer membrane
Topologyout 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 representing this structure 1g90, 2ge4, 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.