Analysis of gating transitions among the three major open states of the OpdK channel

Belete R. Cheneke, Bert Van Den Berg, Liviu Movileanu

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

OpdK is an outer membrane protein of the pathogenic bacterium Pseudomonas aeruginosa. The recent crystal structure of this protein revealed a monomeric, 18-stranded β-barrel with a kidney-shaped pore, whose constriction features a diameter of 8 Å. Using systematic single-channel electrical recordings of this protein pore reconstituted into planar lipid bilayers under a broad range of ion concentrations, we were able to probe its discrete gating kinetics involving three major and functionally distinct conformations, in which a dominant open substate O 2 is accompanied by less thermodynamically stable substates O 1 and O 3. Single-channel electrical data enabled us to determine the alterations in the energetics and kinetics of the OpdK protein when experimental conditions were changed. In the future, such a semiquantitative analysis might provide a better understanding on the dynamics of current fluctuations of other β-barrel membrane protein channels.

Original languageEnglish (US)
Pages (from-to)4987-4997
Number of pages11
JournalBiochemistry
Volume50
Issue number22
DOIs
StatePublished - Jun 7 2011

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Membrane Proteins
Porins
Lipid bilayers
Kinetics
Lipid Bilayers
Ion Channels
Constriction
Pseudomonas aeruginosa
Conformations
Bacteria
Proteins
Crystal structure
Ions
Kidney

ASJC Scopus subject areas

  • Biochemistry

Cite this

Analysis of gating transitions among the three major open states of the OpdK channel. / Cheneke, Belete R.; Van Den Berg, Bert; Movileanu, Liviu.

In: Biochemistry, Vol. 50, No. 22, 07.06.2011, p. 4987-4997.

Research output: Contribution to journalArticle

Cheneke, Belete R. ; Van Den Berg, Bert ; Movileanu, Liviu. / Analysis of gating transitions among the three major open states of the OpdK channel. In: Biochemistry. 2011 ; Vol. 50, No. 22. pp. 4987-4997.
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