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Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli
Yafei Huang,*M. Joanne Lemieux,*Jinmei Song,Manfred Auer,Da-Neng Wang
The major facilitator superfamily represents the largest groupof secondary membrane transporters in the cell. Here we reportthe 3.3 angstrom resolution structure of a member of this superfamily,GlpT, which transports glycerol-3-phosphate into the cytoplasmand inorganic phosphate into the periplasm. The amino- and carboxyl-terminalhalves of the protein exhibit a pseudo two-fold symmetry. Closedoff to the periplasm, a centrally located substrate-translocationpore contains two arginines at its closed end, which comprisethe substrate-binding site. Upon substrate binding, the proteinadopts a more compact conformation. We propose that GlpT operatesby a singlebinding site, alternating-access mechanismthrough 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.
Present address: Department of Biochemistry, University of Alberta,Edmonton, Canada T6G 2H6.
To whom correspondence should be addressed. E-mail: wang{at}saturn.med.nyu.edu
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