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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Veröffentlicht in: | Journal of molecular biology 2007-09, Vol.372 (3), p.565-570 |
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description | 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. |
doi_str_mv | 10.1016/j.jmb.2007.06.067 |
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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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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 |
title | Rigidity of the Subunit Interfaces of the Trimeric Glutamate Transporter GltT During Translocation |
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