Abstract
Several features of ion-channel-forming colicins have been illuminated by recent revelations: its four-domain structure, the mechanism and thermodynamics of binding to the gating loop of outer membrane porins, the mechanism of translocation, competition for the transperiplasmic excursion facilitated by the Tol or Ton transperiplasmic proteins, and the formation of a waisted, funnel-shaped transmembrane channel of well-characterized shape.
Comment
A brief review of the structure of the bacteriocin colicin Ia. This was a structure that had bedevilled many a graduate student and postdoc in the Stroud lab, until finally it was determined by Michael Wiener (now at the University of Virginia). This is a remarkable structure - as Bob Stroud terms it 'the mighty javelin'.