NDLI: Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems

Content Provider	PubMed Central
Author	Angelis, Fabien De Lee, John K. O'connell, Joseph D. Miercke, Larry J. W. Verschueren, Koen H. Srinivasan, Vasundara Bauvois, Cédric Govaerts, Cédric Robbins, Rebecca A. Ruysschaert, Jean-marie Stroud, Robert M. Vandenbussche, Guy
Abstract	Resistance nodulation cell division (RND)-based efflux complexes mediate multidrug and heavy-metal resistance in many Gram-negative bacteria. Efflux of toxic compounds is driven by membrane proton/substrate antiporters (RND protein) in the plasma membrane, linked by a membrane fusion protein (MFP) to an outer-membrane protein. The three-component complex forms an efflux system that spans the entire cell envelope. The MFP is required for the assembly of this complex and is proposed to play an important active role in substrate efflux. To better understand the role of MFPs in RND-driven efflux systems, we chose ZneB, the MFP component of the ZneCAB heavy-metal efflux system from Cupriavidus metallidurans CH34. ZneB is shown to be highly specific for Zn2+ alone. The crystal structure of ZneB to 2.8 Å resolution defines the basis for metal ion binding in the coordination site at a flexible interface between the β-barrel and membrane proximal domains. The conformational differences observed between the crystal structures of metal-bound and apo forms are monitored in solution by spectroscopy and chromatography. The structural rearrangements between the two states suggest an active role in substrate efflux through metal binding and release.
Related Links	http://dx.doi.org/10.1073/pnas.1003908107
Ending Page	11043
Page Count	6
Starting Page	11038
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	107
Language	English
Publisher	National Academy of Sciences
Publisher Date	2010-06-15
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport

pH-induced Conformational Changes of AcrA, the Membrane Fusion Protein of Escherichia coli Multidrug Efflux System

Simulations and Electrostatic Analysis Suggest an Active Role for DNA Conformational Changes During Genome Packaging by Bacteriophages

Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusion

The conformational basis of energy transformations in membrane systems. I. Conformational changes in mitochondria.

Stochastic Fusion Simulations and Experiments Suggest Passive and Active Roles of Hemagglutinin during Membrane Fusion

Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion.

Nisin-induced changes in Bacillus morphology suggest a paradigm of antibiotic action

Role of conformational changes in the elution of proteins from reversed-phase HPLC columns.

Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems

Similar Documents

Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport

pH-induced Conformational Changes of AcrA, the Membrane Fusion Protein of Escherichia coli Multidrug Efflux System

Simulations and Electrostatic Analysis Suggest an Active Role for DNA Conformational Changes During Genome Packaging by Bacteriophages

Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusion

The conformational basis of energy transformations in membrane systems. I. Conformational changes in mitochondria.

Stochastic Fusion Simulations and Experiments Suggest Passive and Active Roles of Hemagglutinin during Membrane Fusion

Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion.

Nisin-induced changes in Bacillus morphology suggest a paradigm of antibiotic action

Role of conformational changes in the elution of proteins from reversed-phase HPLC columns.

Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems