TolQ: Difference between revisions
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TolQ is a polytopic protein located in the inner (cytoplasmic) membrane. It contains approximately 230 amino acids and is important in the maintenance of the bacterial envelope integrity as well as the import of filamentous bacteriophage and group A colicins. <ref name='Vianney'> Vianney A, Lewin TM, Beyer WF Jr, Lazzaroni JC, Portalier R, Webster RE. Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J Bacteriol. 1994 Feb;176(3):822-9</ref> | TolQ is a polytopic protein located in the inner (cytoplasmic) membrane. It contains approximately 230 amino acids and is important in the maintenance of the bacterial envelope integrity as well as the import of filamentous bacteriophage and group A colicins. <ref name='Vianney'> Vianney A, Lewin TM, Beyer WF Jr, Lazzaroni JC, Portalier R, Webster RE. Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J Bacteriol. 1994 Feb;176(3):822-9 PMID:8300535</ref> | ||
==Structure== | ==Structure== | ||
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[[Image:TolQ.jpg|400px|right|thumb| The TolQ Membrane-spanning domains <ref>PMID: 8662905</ref>]] | [[Image:TolQ.jpg|400px|right|thumb| The TolQ Membrane-spanning domains <ref>PMID: 8662905</ref>]] | ||
It has been shown that 4 to 6 TolQ molecules associate in the TolQRA complex, and that they form multimers which interact with the transmembrane helices (TMH) of TolQ, TolR and TolA <ref> PMID: 21285349</ref>. The multimers are formed by the three TMHs <ref name='Vianney'> Vianney A, Lewin TM, Beyer WF Jr, Lazzaroni JC, Portalier R, Webster RE. Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J Bacteriol. 1994 Feb;176(3):822-9</ref> of TolQ, the last of which undergo a conformational change to form a hairpin, while the first TMH forms an intermolecular interaction | It has been shown that 4 to 6 TolQ molecules associate in the TolQRA complex, and that they form multimers which interact with the transmembrane helices (TMH) of TolQ, TolR and TolA <ref> PMID: 21285349</ref>. The multimers are formed by the three TMHs <ref name='Vianney'> Vianney A, Lewin TM, Beyer WF Jr, Lazzaroni JC, Portalier R, Webster RE. Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity. J Bacteriol. 1994 Feb;176(3):822-9 PMID:8300535</ref> of TolQ, the last of which undergo a conformational change to form a hairpin, while the first TMH forms an intermolecular interaction | ||
==To view related Tol entries see:== | ==To view related Tol entries see:== | ||
