A lipid-dependent link between activity and oligomerization state of the M. 
tuberculosis SMR protein TBsmr

Mörs, Karsten; Hellmich, Ute A.; Basting, Daniel; Marchand, Philipp; Wurm, Jan Philip; Haase, Winfried; Glaubitz, Clemens

doi:10.1016/j.bbamem.2012.10.020

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A lipid-dependent link between activity and oligomerization state of the M. tuberculosis SMR protein TBsmr

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Haase, Winfried
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Mörs, K., Hellmich, U. A., Basting, D., Marchand, P., Wurm, J. P., Haase, W., et al. (2013). A lipid-dependent link between activity and oligomerization state of the M. tuberculosis SMR protein TBsmr. Biochimica et Biophysica Acta-Biomembranes, 1828(2), 561-567. doi:10.1016/j.bbamem.2012.10.020.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-D507-7

Zusammenfassung

TBsmr is a secondary active multidrug transporter from Mycobacterium tuberculosis that transports a plethora of compounds including antibiotics and fluorescent dyes. It belongs to the small multidrug resistance (SMR) superfamily and is structurally and functionally related to E. coli EmrE. Of particular importance is the link between protein function, oligomeric state and lipid composition. By freeze fracture EM, we found three different size distributions in three different lipid environments for TBsmr indicating different oligomeric states. The link of these states with protein activity has been probed by fluorescence spectroscopy revealing significant differences. The drug binding site has been probed further by <suo>19</sup>F-MAS NMR through chemical labeling of native cysteine residues showing a water accessible environment in agreement with the alternating access model.