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Structure paper

TitleMechanism of ligand-gated potassium efflux in bacterial pathogens.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 107, Page 19784-19789, Year 2010
Publish dateJan 5, 2010 (structure data deposition date)
AuthorsRoosild, T.P. / Castronovo, S. / Healy, J. / Miller, S. / Pliotas, C. / Rasmussen, T. / Bartlett, W. / Conway, S.J. / Booth, I.R.
External linksProc. Natl. Acad. Sci. USA / PubMed:21041667
MethodsX-ray diffraction
Resolution1.75 - 2.1 Å
Structure data

PDB-3l9w:
KefC C-terminal domain in complex with KefF and GSH
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-3l9x:
KefC C-terminal domain in complex with KefF and ESG
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-ZN:
Unknown entry

ChemComp-GSH:
GLUTATHIONE

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ESG:
L-gamma-glutamyl-S-[(3S)-1-ethyl-2,5-dioxopyrrolidin-3-yl]-L-cysteinylglycine

ChemComp-L9X:
L-gamma-glutamyl-S-[(3R)-1-ethyl-2,5-dioxopyrrolidin-3-yl]-L-cysteinylglycine

Source
  • escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN / potassium channel regulation / potassium efflux / glutathione / KTN(RCK) domains / Antiport / Cell inner membrane / Cell membrane / Ion transport / Membrane / Potassium / Potassium transport / Transmembrane / Transport

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