TolB: Difference between revisions
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The distal N-terminal 12 residues of TolB has two conformational states which are governed by protein-protein interactions with the β -propeller and results in the binding of TolA in the inner membrane.<ref>PMID: 19696740</ref> | The distal N-terminal 12 residues of TolB has two conformational states which are governed by protein-protein interactions with the β -propeller and results in the binding of TolA in the inner membrane.<ref>PMID: 19696740</ref> | ||
TolB has been shown to interact with the porins of Escherichia coli, in particular OmpF, OmpC, PhoE and LamB, but not OmpA or any of their denatured counterparts<ref>PMID: 9393690</ref> | TolB has been shown to interact with the porins of Escherichia coli, in particular OmpF, OmpC, PhoE and LamB, but not OmpA or any of their denatured counterparts. It has been proposed that the whole Tol complex plays a role in this association, although "tol" mutants do not prevent this assembly completely therefore the Tol system may be involved kinetically, not directly.<ref>PMID: 9393690</ref> | ||
==The TolB-Pal Complex== | ==The TolB-Pal Complex== | ||
