1887

Abstract

Native and recombinant FomA proteins were extracted by detergent from the cell envelopes of and , and purified to near homogeneity by chromatography. Circular dichroism analysis revealed that the FomA protein consists predominantly of β-sheets, in line with the previously proposed 16-stranded β-barrel topology model. Results obtained by trypsin treatment of intact cells and cell envelopes of , and from limited proteolysis of purified FomA protein, indicated that the N-terminal part of the FomA protein is not an integral part of the β-barrel, but forms a periplasmic domain. Based on these results a new topology model is proposed for the FomA protein, where the C-terminal part forms a 14-stranded β-barrel separate from the periplasmic N-terminal domain.

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2002-11-01
2020-09-29
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