Structural basis of Na+-independent and cooperative substrate/product antiport in CaiT

Transport proteins: sodium-free protein exchange Transport of solutes across biological membranes is carried out by specialized secondary transport proteins in the lipid bilayer. In this paper, the authors report the structures of the sodium-independent membrane antiporter CaiT isolated from two mic...

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Veröffentlicht in:	Nature (London) 2010-09, Vol.467 (7312), p.233-236
Hauptverfasser:	Schulze, Sabrina, Köster, Stefan, Geldmacher, Ulrike, Terwisscha van Scheltinga, Anke C., Kühlbrandt, Werner
Format:	Artikel
Sprache:	eng
Schlagworte:	631/337 631/45/535 631/57/2270/1140 Antiporters - chemistry Antiporters - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Betaine - analogs & derivatives Betaine - metabolism Biochemistry Biological and medical sciences Biological membranes Biological Transport Carnitine - metabolism Crystalline structure E coli Enzymes Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Hydrogen bonds letter Models, Molecular Molecular biophysics multidisciplinary Mutation Proteins Proteus mirabilis - metabolism Science Science (multidisciplinary) Solutes Structure in molecular biology Substrates Translocation
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