Rigidity of the subunit interfaces of the trimeric glutamate transporter GltT during translocation

Maarten Groeneveld; Dirk-Jan Slotboom

doi:10.1016/j.jmb.2007.06.067

Rigidity of the subunit interfaces of the trimeric glutamate transporter GltT during translocation

J Mol Biol. 2007 Sep 21;372(3):565-70. doi: 10.1016/j.jmb.2007.06.067. Epub 2007 Jun 29.

Authors

Maarten Groeneveld¹, Dirk-Jan Slotboom

Affiliation

¹ Department of Biochemistry, University of Groningen, Groningen Biomolecular Science and Biotechnology Institute, Nijenborgh 4, 9747 AG Groningen, The Netherlands.

PMID: 17673229
DOI: 10.1016/j.jmb.2007.06.067

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Transport Systems, Acidic / chemistry*
Amino Acid Transport Systems, Acidic / metabolism*
Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism*
Biological Transport
Disulfides
Geobacillus stearothermophilus / metabolism*
Glutamic Acid / metabolism*
Models, Molecular
Mutant Proteins / metabolism
Protein Structure, Quaternary
Protein Subunits / chemistry*
Protein Subunits / metabolism*
Symporters / chemistry*
Symporters / metabolism*

Substances

Amino Acid Transport Systems, Acidic
Bacterial Proteins
Disulfides
Mutant Proteins
Protein Subunits
Symporters
gltT protein, Bacillus stearothermophilus
Glutamic Acid