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Stability of Trimeric OmpF Porin:  The Contributions of the Latching Loop L2

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Divisions of Microbiology, Structural Biology and Biophysical Chemistry, Biozentrum, University of Basel, CH-4056 Basel, Switzerland
Cite this: Biochemistry 1998, 37, 45, 15663–15670
Publication Date (Web):October 20, 1998
Copyright © 1998 American Chemical Society

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    The channel-forming protein OmpF porin from Escherichia coli spans the bacterial outer membrane. Each of the three monomers comprises a hollow, 16-stranded β-barrel. These are associated to homotrimers which are unusually stable, due mostly to hydrophobic interactions between the β-barrels. In addition, a loop, L2 connects one subunit to its neighbor by latching into its channel. Residue E71 on loop 2 is integrated into an ionic network and forms salt bridges and hydrogen bonds with R100 and R132 on the channel wall in the adjacent subunit. To examine these contributions quantitatively, six single-site, two double, and one deletion mutant were constructed on the basis of the atomic coordinates of the protein. Differential scanning calorimetric analysis showed that the salt-bridge, E71-R100, contributes significantly to trimer stability:  the substitution E71Q causes a decrease of the transition temperature from 72 to 48 °C, with ΔHcal diminishing from 430 to 201 kcal mol-1. A nearby substitution in the loop, D74N, has lesser effects on thermal stability, while the deletion in L2 (Δ69−77) has an effect comparable to that of E71Q. X-ray structure analysis to 3.0 Å resolution revealed only local structural differences in the mutants except for the substitution R100A, where another residue, R132, is found to fill the gap left by the truncated side chain of A100. Functional assays in planar lipid bilayers show significantly increased cation selectivities if the charge distribution was affected.

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     This work was supported by grants from the Swiss National Science Foundation to J.P.R. and T.S. and by support from EU-BIOTECH/BBW to J.P.R.

     Division of Microbiology.


     Division of Structural Biology.

     Division of Biophysical Chemistry.


     To whom correspondence should be addressed. E-mail:  [email protected].

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    Determination of ΔCp by monitoring pH dependent changes in the ΔHcal and Tm for wild-type, E71A, and E71Q mutants of OmpF are presented together with two figures and one table (6 pages). Ordering information is given on any current masthead page.

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