期刊
SCIENCE
卷 321, 期 5890, 页码 810-814出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1160406
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资金
- NIDDK NIH HHS [R01 DK019567, DK19567, R01 DK044602, DK44602] Funding Source: Medline
- NIGMS NIH HHS [R01 GM078844, R01 GM078844-01, R01 GM078844-02, R01 GM078844-03, GM07844] Funding Source: Medline
Membrane transporters that use energy stored in sodium gradients to drive nutrients into cells constitute a major class of proteins. We report the crystal structure of a member of the solute sodium symporters (SSS), the Vibrio parahaemolyticus sodium/galactose symporter (vSGLT). The similar to 3.0 angstrom structure contains 14 transmembrane (TM) helices in an inward-facing conformation with a core structure of inverted repeats of 5 TM helices (TM2 to TM6 and TM7 to TM11). Galactose is bound in the center of the core, occluded from the outside solutions by hydrophobic residues. Surprisingly, the architecture of the core is similar to that of the leucine transporter (LeuT) from a different gene family. Modeling the outward-facing conformation based on the LeuT structure, in conjunction with biophysical data, provides insight into structural rearrangements for active transport.
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