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

  • Juan Fernández-Recio (Contributor)
  • Rajeev Misra (Contributor)
  • Zbigniew Pietras (Contributor)
  • Vassiliy N. Bavro (Contributor)
  • Vassiliy N. Bavro (Contributor)
  • Laura Pérez-Cano (Contributor)
  • Nicholas Furnham (Contributor)
  • Rajeev Misra (Contributor)
  • Ben Luisi (Contributor)
  • Xue Yuan Pei (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.3
Classification:TRANSPORT PROTEIN
Release Date:2008-04-22
Deposition Date:2007-10-04
Revision Date:2011-05-08#2011-07-13#2018-01-24
Molecular Weight:152092.66
Macromolecule Type:Protein
Residue Count:1380
Atom Site Count:9914
DOI:10.2210/pdb2vdd/pdb

Abstract:
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.
Date made availableApr 22 2008
PublisherRCSB-PDB

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