ArticleBiophysical journal2006
Changes in secondary structures and acidic side chains of melibiose permease upon cosubstrates binding.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Reduced Na+ affinity increases turnover of Salmonella enterica serovar Typhimurium MelB.Journal of bacteriology · 2012Article
- Role of Gly117 in the cation/melibiose symport of MelB of Salmonella typhimurium.Biochemistry · 2012Article
- Mechanism of melibiose/cation symport of the melibiose permease of Salmonella typhimurium.The Journal of biological chemistry · 2011Article
- Structural insights into the activation mechanism of melibiose permease by sodium binding.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- A 3D structure model of the melibiose permease of Escherichia coli represents a distinctive fold for Na+ symporters.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Alteration of sugar-induced conformational changes of the melibiose permease by mutating Arg141 in loop 4-5.Biophysical journal · 2009Article
- FTIR spectroscopy of secondary-structure reorientation of melibiose permease modulated by substrate binding.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infrared difference spectroscopy analysis of the purified melibiose permease of Escherichia coli reconstituted into liposomes was carried out as a function of the presence of the two symporter substrates (Na(+), melibiose) in either H(2)O or in D(2)O media. Essentially, the data first show that addition of Na(+) induces appearance of peaks assigned to changes in the environment and/or orientation of alpha-helical domains of purified melibiose permease. Likewise, melibiose addition in the presence of Na(+) produces peaks corresponding to additional changes of alpha-helix environment or tilt. In addition to these changes, a pair of peaks (1599 (+) cm(-1)/1576 (-) cm(-1)) appearing in the Na(+)-induced difference spectrum is assigned to the antisymmetric stretching of COO(-) groups, since they show practically no shift upon H/D exchange. It is proposed that these acidic groups participate in Na(+) co-ordination. A corresponding pair of peaks, again fairly insensitive to H/D substitution (1591 (-) cm(-1)/1567 (+) cm(-1)), appear in the melibiose-induced difference spectra, and may again be assigned to COO(-) groups. The latter carboxyl groups may correspond to part or all of the acidic residues interacting with Lys or Arg in the resting state that become free upon melibiose binding.
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