2VDD: Crystal Structure of the Open State of TolC Outer Membrane Component of Mutlidrug Efflux Pumps

Drugs and certain proteins are transported across the membranes of Gram-negative bacteria by energy-activated pumps. The outer membrane component of these pumps is a channel that opens from a sealed resting state during the transport process. We describe two crystal structures of the Escherichia coli outer membrane protein TolC in its partially open state. Opening is accompanied by the exposure of three shallow intraprotomer grooves in the TolC trimer, where our mutagenesis data identify a contact point with the periplasmic component of a drug efflux pump, AcrA. We suggest that the assembly of multidrug efflux pumps is accompanied by induced fit of TolC driven mainly by accommodation of the periplasmic component.
PDB ID: 2VDDDownload
MMDB ID: 63944
PDB Deposition Date: 2007/10/4
Updated in MMDB: 2011/10
Experimental Method:
x-ray diffraction
Resolution: 3.3  Å
Source Organism:
Similar Structures:
Biological Unit for 2VDD: trimeric; determined by author and by software (PQS)
Molecular Components in 2VDD
Label Count Molecule
Proteins (3 molecules)
Outer Membrane Protein Tolc(Gene symbol: tolC)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB