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Science 1 August 2003:
Vol. 301. no. 5633, pp. 616 - 620
DOI: 10.1126/science.1087619
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Research Articles

Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli

Yafei Huang,* M. Joanne Lemieux,*{dagger} Jinmei Song, Manfred Auer, Da-Neng Wang{ddagger}

The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single–binding site, alternating-access mechanism through a rocker-switch type of movement.

Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.


* These authors contributed equally to this work.

{dagger} Present address: Department of Biochemistry, University of Alberta, Edmonton, Canada T6G 2H6.

{ddagger} To whom correspondence should be addressed. E-mail: wang{at}saturn.med.nyu.edu

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