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. 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.
Department of Biochemistry, University of Groningen, Groningen Biomolecular Science and Biotechnology Institute, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Maarten
M
Groeneveld
Dirk-Jan
DJ
Slotboom
D026922:Amino Acid Transport Systems, Acidic / Q000737:chemistry* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001692:Biological Transport; D004220:Disulfides; D001411:Geobacillus stearothermophilus / Q000378:metabolism*; D018698:Glutamic Acid / Q000378:metabolism*; D008958:Models, Molecular; D050505:Mutant Proteins / Q000378:metabolism; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry* / Q000378:metabolism*; D027981:Symporters / Q000737:chemistry* / Q000378:metabolism*
D026922:Amino Acid Transport Systems, Acidic; D001426:Bacterial Proteins; D004220:Disulfides; D050505:Mutant Proteins; D021122:Protein Subunits; D027981:Symporters; C077709:gltT protein, Bacillus stearothermophilus; D018698:Glutamic Acid