3DH4

Crystal Structure of Sodium/Sugar symporter with bound Galactose from vibrio parahaemolyticus

Summary for 3DH4

• Entry DOI: 10.2210/pdb3dh4/pdb
• Descriptor: Sodium/glucose cotransporter, beta-D-galactopyranose, ERBIUM (III) ION, ... (4 entities in total)
• Functional Keywords: membrane protein, symporter, sugar transport, sglt, ion transport, membrane, sodium transport, symport, transmembrane, transport, transport protein
• Biological source: Vibrio parahaemolyticus
• Cellular location: Cell membrane; Multi-pass membrane protein: P96169
• Total number of polymer chains: 4
• Total formula weight: 229217.12

Authors

Abramson, J.,Faham, S.,Cascio, D. (deposition date: 2008-06-16, release date: 2008-08-05, Last modification date: 2024-02-21)

Primary citation

Faham, S.,Watanabe, A.,Besserer, G.M.,Cascio, D.,Specht, A.,Hirayama, B.A.,Wright, E.M.,Abramson, J.
The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport.
Science, 321:810-814, 2008

PubMed Abstract: 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 approximately 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.

PubMed: 18599740
DOI: 10.1126/science.1160406

Experimental method

X-RAY DIFFRACTION (2.7 Å)