Structure-function of cyanobacterial outer-membrane protein, Slr1270: Homolog of Escherichia coli drug export/colicin import protein, TolC

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Abstract

Compared to thylakoid and inner membrane proteins in cyanobacteria, no structure-function information is available presently for integral outer-membrane proteins (OMPs). The Slr1270 protein from the cyanobacterium Synechocystis 6803, over-expressed in Escherichia coli, was refolded, and characterized for molecular size, secondary structure, and ion-channel function. Refolded Slr1270 displays a single band in native-electrophoresis, has an α-helical content of 50-60%, as in E. coli TolC with which it has significant secondary-structure similarity, and an ion-channel function with a single-channel conductance of 80-200 pS, and a monovalent ion (K+:Cl-) selectivity of 4.7:1. The pH-dependence of channel conductance implies a role for carboxylate residues in channel gating, analogous to that in TolC. 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Agarwal, R., Zakharov, S., Hasan, S. S., Ryan, C. M., Whitelegge, J. P., & Cramer, W. A. (2014). Structure-function of cyanobacterial outer-membrane protein, Slr1270: Homolog of Escherichia coli drug export/colicin import protein, TolC. FEBS Letters, 588(21), 3793–3801. https://doi.org/10.1016/j.febslet.2014.08.028

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