PDBsum entry 2f1v

Membrane protein

PDB id: 2f1v

Contents

Protein chains

(+ 0 more) 182 a.a. *

Ligands

GOL ×6

* Residue conservation analysis

PDB id:

2f1v

Name:

Membrane protein

Title:

Outer membrane protein ompw

Structure:

Outer membrane protein w. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Escherichia coli k12. Organism_taxid: 83333. Strain: k-12. Gene: ompw. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.70Å R-factor: 0.292 R-free: 0.314

Authors:

B.Van Den Berg

Key ref:

H.Hong et al. (2006). The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel. J Biol Chem, 281, 7568-7577. PubMed id: 16414958 DOI: 10.1074/jbc.M512365200

Date:

15-Nov-05 Release date: 24-Jan-06

Protein chains

P0A915  (OMPW_ECOLI) -  Outer membrane protein W from Escherichia coli (strain K12)

Seq: 212 a.a.

Struc: 182 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M512365200

J Biol Chem 281:7568-7577 (2006)

PubMed id: 16414958

The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel.

H.Hong, D.R.Patel, L.K.Tamm, B.van den Berg.

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.

Selected figure(s)

Figure 1.
FIGURE 1. Schematic overview of the OmpW structure. A and B, ribbon diagrams viewed from the side, with B, 90° rotated relative to A. Extracellular loops (L) and periplasmic turns (T) are indicated. The N terminus in B is indicated with N, and the C terminus is indicated with C. The -strands are numbered from S1 to S8. The position of the opening in the barrel wall between strands S3 and S4 is indicated with an asterisk (^*). The approximate boundary of the hydrophobic part of the OM is indicated with horizontal lines, with out being the extracellular environment and in the periplasmic space. C, view of OmpW from the extracellular side, showing the ellipsoid shape of the barrel. The positions of several loops are indicated. Figs. 1, 3, and 8 were generated with PYMOL (40).

Figure 4.
FIGURE 4. Representative single channel recordings of OmpW, OmpA, and Tsx in planar diphytanoyl-PC lipid bilayers in 1 M KCl at pH 7 and +140 mV. Proteins were reconstituted from C[8]E[4] detergent micelles or DPPC (DPoPC) proteoliposomes as indicated.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 7568-7577) copyright 2006.

Figures were selected by an automated process.