2vdd
From Proteopedia
CRYSTAL STRUCTURE OF THE OPEN STATE OF TOLC OUTER MEMBRANE COMPONENT OF MUTLIDRUG EFFLUX PUMPS
Overview
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.
About this Structure
2VDD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Assembly and channel opening in a bacterial drug efflux machine., Bavro VN, Pietras Z, Furnham N, Perez-Cano L, Fernandez-Recio J, Pei XY, Misra R, Luisi B, Mol Cell. 2008 Apr 11;30(1):114-21. PMID:18406332 Page seeded by OCA on Thu Apr 24 09:42:50 2008
Categories: Escherichia coli | Single protein | Bavro, V N. | Fernandez-Recio, J. | Furnham, N. | Luisi, B. | Misra, R. | Pei, X Y. | Perez-Cano, L. | Pietras, Z. | Truer, R. | Alpha helical barrel | Beta barrel | Integral membrane protein | Membrane | Multidrug efflux pump | Outer membrane | Transmembrane | Transport | Transport protein
