Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel

Gina M. Clayton, Steve Altieri, Lise Heginbotham, Vinzenz M. Unger, João H. Morais-Cabral

Research output: Contribution to journalArticlepeer-review

140 Scopus citations


The six-transmembrane helix (6 TM) tetrameric cation channels form the largest ion channel family, some members of which are voltage-gated and others are not. There are no reported channel structures to match the wealth of functional data on the nonvoltage-gated members. We determined the structure of the transmembrane regions of the bacterial cyclic nucleotide-regulated channel MlotiK1, a non-voltage-gated 6 TM channel. The structure showed how the S1-S4 domain and its associated linker can serve as a clamp to constrain the gate of the pore and possibly function in concert with ligand-binding domains to regulate the opening of the pore. The structure also led us to hypothesize a new mechanism by which motions of the S6 inner helices can gate the ion conduction pathway at a position along the pore closer to the selectivity filter than the canonical helix bundle crossing.

Original languageEnglish (US)
Pages (from-to)1511-1515
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number5
StatePublished - Feb 5 2008


  • Crystal structure
  • Membrane protein
  • Non-voltage-gated

ASJC Scopus subject areas

  • General


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