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TitleKTN (RCK) Domains Regulate K(+) Channels and Transporters by Controlling the Dimer-Hinge Conformation.
Journal, issue, pagesStructure, Vol. 17, Page 893-903, Year 2009
Publish dateOct 22, 2008 (structure data deposition date)
AuthorsRoosild, T.P. / Castronovo, S. / Miller, S. / Li, C. / Rasmussen, T. / Bartlett, W. / Gunasekera, B. / Choe, S. / Booth, I.R.
External linksStructure / PubMed:19523906
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-3eyw:
Crystal structure of the C-terminal domain of E. coli KefC in complex with KefF
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / KTN / RCK / K+ channel / K+ transport / KefC / K+ efflux / channel regulation / Antiport / Inner membrane / Ion transport / Membrane / Potassium / Potassium transport / Transmembrane

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