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• W2037926721 abstract "The bacterial Na+/galactose cotransporter vSGLT of Vibrio parahaemolyticus is a member of the sodium:solute symporter family (SSS). Previous studies using electron microscopy have shown that vSGLT is a monomeric protein. Computational and experimental topological analyses have consistently indicated that this protein possesses 14 transmembrane α-helices. Our previous study using attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR) to quantitate secondary structure content had indicated, in contrast, an α-helical content of only 35%, too little to be consistent with the 14-span model [le Coutre, J., et al. (2002) Biochemistry 41, 8082−6]. ATR-FTIR had also indicated that upon binding of Na+ and d-galactose, the α-helical content increased to 53%. Here we revisit the vSGLT secondary structural distribution using an alternative approach, ultraviolet circular dichroism spectropolarimetry (CD), which is highly accurate in determining the α-helical content of a protein in solution. CD spectra were obtained from actively functional, soluble vSGLT and, as an internal check, from a fusion protein of vSGLT and the β-barrel green fluorescent protein (GFP). Far-UV CD of vSGLT indicates a predominating 85% α-helical content, and an absence of β-strands. Far-UV CD of the vSGLT−GFP fusion corroborates this profile, indicating an equivalent α-helical content, and a β-strand content consistent with the GFP contribution. No detectable substrate-induced macroscopic changes in secondary structure are apparent in the far UV. In the near UV, increases in positive CD intensity occur in a stepwise manner with added substrates, implying changing environments of aromatic amino acid residues. CD thus confirms the current 14-transmembrane span model of vSGLT and reveals distinct substrate-induced conformational changes. The high percentage of α-helical structure found requires, when considered in the context of membrane topology, that nearly a third of the total α-helical fraction lies in extramembrane domains, which distinguishes this cotransporter from the unrelated lactose and glycerol 3-phosphate transporters." @default.
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• W2037926721 date "2006-01-11" @default.
• W2037926721 modified "2023-09-28" @default.
• W2037926721 title "A Reinvestigation of the Secondary Structure of Functionally Active vSGLT, the<i> Vibrio</i> Sodium/Galactose Cotransporter" @default.
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• W2037926721 doi "https://doi.org/10.1021/bi052160z" @default.
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