کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1944393 | 1053210 | 2013 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A lipid-dependent link between activity and oligomerization state of the M. tuberculosis SMR protein TBsmr A lipid-dependent link between activity and oligomerization state of the M. tuberculosis SMR protein TBsmr](/preview/png/1944393.png)
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 19F-MAS NMR through chemical labeling of native cysteine residues showing a water accessible environment in agreement with the alternating access model.
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► The link between lipid-induced oligomerization and function of the SMR protein TBsmr is investigated.
► Lipid bilayer bulk properties determine TBsmr transport activity and oligomerization.
► 19F Solid State NMR data indicate a water-filled pore for the binding pocket.
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1828, Issue 2, February 2013, Pages 561–567