Abstract
A 53-kDa protein from the outer sheath of the oral spirochete Treponema denticola was purified to homogeneity and shown to reconstitute channels in black lipid bilayer model membranes. The channel had a single-channel conductance of 1.8 nS in 0.1 M KCl, making this the largest porin channel observed to date (estimated diameter, 3.4 nm). Electron micrographs of 53-kDa-protein-containing outer sheaths of T. denticola showed a regular hexagonal array of darker staining pits.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, Bacterial / chemistry*
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Antigens, Surface / chemistry*
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Bacterial Adhesion
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Bacterial Outer Membrane Proteins / chemistry*
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Electric Conductivity
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Ion Channel Gating
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Ion Channels / chemistry*
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Membranes, Artificial
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Microscopy, Electron
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Molecular Weight
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Porins
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Treponema / chemistry*
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Treponema / ultrastructure
Substances
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Antigens, Bacterial
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Antigens, Surface
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Bacterial Outer Membrane Proteins
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Ion Channels
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Membranes, Artificial
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Porins