The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport

被引:430
作者
Faham, Salem [1 ]
Watanabe, Akira [1 ]
Besserer, Gabriel Mercado [1 ]
Cascio, Duilio [2 ]
Specht, Alexandre [3 ]
Hirayama, Bruce A. [1 ]
Wright, Ernest M. [1 ]
Abramson, Jeff [1 ]
机构
[1] Univ Calif Los Angeles, Dept Physiol, David Geffen Sch Med, Los Angeles, CA 90095 USA
[2] Univ Calif Los Angeles, UCLA Dept Energy Inst Genom & Proteom, Los Angeles, CA 90095 USA
[3] Univ Strasbourg 1, Chim Bioorgan Lab, CNRS, Fac Pharm,UMR 7175, F-67401 Illkirch Graffenstaden, France
关键词
D O I
10.1126/science.1160406
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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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页码:810 / 814
页数:5
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