2VDD

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

Summary for 2VDD

• Entry DOI: 10.2210/pdb2vdd/pdb
• Related: 1EK9 1TQQ 1TTQ 2VDE
• Descriptor: OUTER MEMBRANE PROTEIN TOLC, CHLORIDE ION, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: beta barrel, alpha helical barrel, multidrug efflux pump, integral membrane protein, outer membrane, membrane, transport, transmembrane, transport protein
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 3
• Total formula weight: 152092.65

Authors

Bavro, V.N.,Pietras, Z.,Furnham, N.,Perez-Cano, L.,Fernandez-Recio, J.,Pei, X.Y.,Truer, R.,Misra, R.,Luisi, B. (deposition date: 2007-10-04, release date: 2008-04-22, Last modification date: 2023-12-13)

Primary citation

Bavro, V.N.,Pietras, Z.,Furnham, N.,Perez-Cano, L.,Fernandez-Recio, J.,Pei, X.Y.,Truer, R.,Misra, R.,Luisi, B.
Assembly and Channel Opening in a Bacterial Drug Efflux Machine.
Mol.Cell, 30:114-, 2008

PubMed 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.

PubMed: 18406332
DOI: 10.1016/J.MOLCEL.2008.02.015

Experimental method

X-RAY DIFFRACTION (3.3 Å)