Rigidity of the Subunit Interfaces of the Trimeric Glutamate Transporter GltT During Translocation

Glutamate transporters are trimeric membrane proteins in which each protomer contains a separate translocation path. To determine whether structural rearrangements take place at the subunit interfaces during transport, intersubunit disulfide bridges were introduced in the bacterial transporter GltT....

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Bibliographic Details
Published in:Journal of molecular biology 2007-09, Vol.372 (3), p.565-570
Main Authors: Groeneveld, Maarten, Slotboom, Dirk-Jan
Format: Article
Language:English
Subjects:
Amino Acid Transport Systems, Acidic - chemistry
Amino Acid Transport Systems, Acidic - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biological Transport
Disulfides
Geobacillus stearothermophilus - metabolism
glutamate transport
Glutamic Acid - metabolism
membrane protein
Models, Molecular
Mutant Proteins - metabolism
oligomeric state
Protein Structure, Quaternary
Protein Subunits - chemistry
Protein Subunits - metabolism
subunit interaction
Symporters - chemistry
Symporters - metabolism
transport mechanism
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Summary:Glutamate transporters are trimeric membrane proteins in which each protomer contains a separate translocation path. To determine whether structural rearrangements take place at the subunit interfaces during transport, intersubunit disulfide bridges were introduced in the bacterial transporter GltT. None of the intersubunit cross-links, which had been designed across the entire interface, affected the glutamate transport activity, indicating that the subunit interfaces are rigid during turnover.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2007.06.067