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Literature DB >> 17673229

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

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.

Entities: Chemical Disease

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Year: 2007 PMID： 17673229 DOI： 10.1016/j.jmb.2007.06.067

Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469

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Cited

35 in total

1. Constraints imposed by the membrane selectively guide the alternating access dynamics of the glutamate transporter GltPh.

Authors: Timothy R Lezon; Ivet Bahar
Journal: Biophys J Date: 2012-03-20 Impact factor: 4.033

2. CLC Cl /H+ transporters constrained by covalent cross-linking.

Authors: Wang Nguitragool; Christopher Miller
Journal: Proc Natl Acad Sci U S A Date: 2007-12-18 Impact factor: 11.205

3. Crystal structure of a substrate-free aspartate transporter.

Authors: Sonja Jensen; Albert Guskov; Stephan Rempel; Inga Hänelt; Dirk Jan Slotboom
Journal: Nat Struct Mol Biol Date: 2013-09-08 Impact factor: 15.369

4. Mechanism of transport modulation by an extracellular loop in an archaeal excitatory amino acid transporter (EAAT) homolog.

Authors: Christopher Mulligan; Joseph A Mindell
Journal: J Biol Chem Date: 2013-10-23 Impact factor: 5.157

10. Disulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductance.

Authors: Mustafa Shabaneh; Noa Rosental; Baruch I Kanner
Journal: J Biol Chem Date: 2014-02-28 Impact factor: 5.157

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

1. Constraints imposed by the membrane selectively guide the alternating access dynamics of the glutamate transporter GltPh.

2. CLC Cl /H+ transporters constrained by covalent cross-linking.

3. Crystal structure of a substrate-free aspartate transporter.

4. Mechanism of transport modulation by an extracellular loop in an archaeal excitatory amino acid transporter (EAAT) homolog.

5. Quality control of overexpressed membrane proteins.

6. Penicillin-binding protein 5 can form a homo-oligomeric complex in the inner membrane of Escherichia coli.

7. Large collective motions regulate the functional properties of glutamate transporter trimers.

8. Conformational heterogeneity of the aspartate transporter Glt(Ph).

9. Molecular Determinants of Substrate Specificity in Sodium-coupled Glutamate Transporters.

10. Disulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductance.