• Publications
  • Influence
Transition to the open state of the TolC periplasmic tunnel entrance
The results support a model in which transition to the open state of TolC is achieved by an iris-like realignment of the tunnel entrance helices, generating an aperture that corresponds to the modeled open state, with the capacity to allow access and passage of diverse substrates. Expand
The cell surface expression of group 2 capsular polysaccharides in Escherichia coli: the role of KpsD, RhsA and a multi‐protein complex at the pole of the cell
The KpsD protein, previously believed to be a periplasmic protein, is an outer membrane protein involved in the export of group 2 capsular polysaccharides across the outer membrane and the RhsA protein, of previously unknown function, could be cross‐linked to the complex. Expand
An RND-Type Efflux System in Borrelia burgdorferi Is Involved in Virulence and Resistance to Antimicrobial Compounds
It is shown that BesC, a TolC homolog, forms channels in planar lipid bilayers and is involved in antibiotic resistance, signifying the importance of this outer membrane channel in the mammalian host. Expand
Protein export and drug efflux through bacterial channel-tunnels.
The bacterial protein TolC assembles into an alpha-helical trans-periplasmic tunnel, which is embedded in the outer membrane by a contiguous beta-barrel channel. TolC and its homologues thus provideExpand
An aspartate ring at the TolC tunnel entrance determines ion selectivity and presents a target for blocking by large cations
The function of wild‐type TolC as a membrane pore was severely inhibited by divalent and trivalent cations entering the channel tunnel from the channel (‘extracellular’) side, supporting the view that the aspartate ring is the cation binding site. Expand
Importance of the adaptor (membrane fusion) protein hairpin domain for the functionality of multidrug efflux pumps.
Drug efflux pumps of Gram-negative bacteria are tripartite export machineries located in the bacterial envelopes contributing to multidrug resistance and the interaction of the hairpin domain and the channel tunnel on a molecular level for AcrA and TolC as well as MexA and OprM is modeled. Expand
Electrophysiological Behavior of the TolC Channel-Tunnel in Planar Lipid Bilayers
The electrophysiological behavior of TolC reconstituted into planar lipid bilayers is investigated, in particular the influence of the membrane potential, the electrolyte concentration and pH. Expand
A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins
DsbG is the first member of the dsb family for which null mutations are conditionally lethal and can be propagated only if supplemented with oxidants in the growth medium, and demonstrates that DsbG acts in vivo as an efficient thiol–disulphide oxidase. Expand
Chunnel vision
The crystal structure has revealed that TolC assembles into a remarkable α‐helical trans‐periplasmic cylinder (tunnel) embedded in the outer membrane by a contiguous β‐barrel (channel), so providing a large duct open to the outside environment. Expand
Channel-tunnels: outer membrane components of type I secretion systems and multidrug efflux pumps of Gram-negative bacteria.
  • C. Andersen
  • Chemistry, Medicine
  • Reviews of physiology, biochemistry and…
  • 2003
Channel-tunnels are outer membrane proteins, which are central to two distinct export systems: type I secretion system exporting proteins such as toxins or proteases, and efflux pumps discharging antibiotics, dyes, or heavy metals and thus mediating drug resistance. Expand