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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5633
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pubmed:dateCreated |
2003-8-1
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
301
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
616-20
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:12893936-Amino Acid Sequence,
pubmed-meshheading:12893936-Binding Sites,
pubmed-meshheading:12893936-Biological Transport,
pubmed-meshheading:12893936-Cell Membrane,
pubmed-meshheading:12893936-Crystallization,
pubmed-meshheading:12893936-Crystallography, X-Ray,
pubmed-meshheading:12893936-Escherichia coli,
pubmed-meshheading:12893936-Escherichia coli Proteins,
pubmed-meshheading:12893936-Glycerophosphates,
pubmed-meshheading:12893936-Helix-Turn-Helix Motifs,
pubmed-meshheading:12893936-Mass Spectrometry,
pubmed-meshheading:12893936-Membrane Transport Proteins,
pubmed-meshheading:12893936-Models, Molecular,
pubmed-meshheading:12893936-Molecular Sequence Data,
pubmed-meshheading:12893936-Periplasm,
pubmed-meshheading:12893936-Phosphates,
pubmed-meshheading:12893936-Protein Conformation,
pubmed-meshheading:12893936-Protein Folding,
pubmed-meshheading:12893936-Protein Structure, Secondary,
pubmed-meshheading:12893936-Protein Structure, Tertiary
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pubmed:year |
2003
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pubmed:articleTitle |
Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli.
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pubmed:affiliation |
Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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