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Structure paper

TitleThe occupancy of ions in the K+ selectivity filter: Charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates
Journal, issue, pagesJ. Mol. Biol., Vol. 333, Page 965-975, Year 2003
Publish dateOct 2, 2003 (structure data deposition date)
AuthorsZhou, Y. / MacKinnon, R.
External linksJ. Mol. Biol. / PubMed:14583193
MethodsX-ray diffraction
Resolution1.9 - 2.8 Å
Structure data

PDB-1r3i:
potassium channel KcsA-Fab complex in Rb+
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1r3j:
potassium channel KcsA-Fab complex in high concentration of Tl+
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1r3k:
potassium channel KcsA-Fab complex in low concentration of Tl+
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-1r3l:
potassium channel KcsA-Fab complex in Cs+
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

Chemicals

ChemComp-F09:
NONAN-1-OL

ChemComp-RB:
RUBIDIUM ION

ChemComp-DGA:
DIACYL GLYCEROL

ChemComp-HOH:
WATER

ChemComp-TL:
THALLIUM (I) ION

ChemComp-CS:
Unknown entry

Source
  • streptomyces lividans (bacteria)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / potassium channel / KcsA-Fab complex / rubidium / Thallium / Cesium

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