ArticleBiochemistry2011
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- The battle for silver binding: How the interplay between the SilE, SilF, and SilB proteins contributes to the silver efflux pump mechanism.The Journal of biological chemistry · 2023Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- PcoB is a defense outer membrane protein that facilitates cellular uptake of copper.Protein science : a publication of the Protein Society · 2022Article
- Exploring the role of the various methionine residues in the Escherichia coli CusB adapter protein.PloS one · 2019Article
- Inhibiting the copper efflux system in microbes as a novel approach for developing antibiotics.PloS one · 2019Article
- Resistance to Metals Used in Agricultural Production.Microbiology spectrum · 2018Review
- Trapping intermediates in metal transfer reactions of the CusCBAF export pump ofCommunications biology · 2018Article
- A comprehensive phylogenetic analysis of copper transporting PMicrobiologyOpen · 2017Article
- Adaptor protein mediates dynamic pump assembly for bacterial metal efflux.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding.Biophysical journal · 2017Article
- Article
- AztD, a Periplasmic Zinc Metallochaperone to an ATP-binding Cassette (ABC) Transporter System in Paracoccus denitrificans.The Journal of biological chemistry · 2015Article
- Copper tolerance and virulence in bacteria.Metallomics : integrated biometal science · 2015Review
- Silver resistance in Gram-negative bacteria: a dissection of endogenous and exogenous mechanisms.The Journal of antimicrobial chemotherapy · 2015Article
- CopM is a novel copper-binding protein involved in copper resistance in Synechocystis sp. PCC 6803.MicrobiologyOpen · 2015Article
- Mechanism of coupling drug transport reactions located in two different membranes.Frontiers in microbiology · 2015Review
- Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.Frontiers in microbiology · 2015Review
- Copper transport and trafficking at the host-bacterial pathogen interface.Accounts of chemical research · 2014Article
- Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The Escherichia coli periplasmic proteins CusF and CusB, as part of the CusCFBA efflux system, aid in the resistance of elevated levels of copper and silver by direct metal transfer between the metallochaperone CusF and the membrane fusion protein CusB before metal extrusion from the periplasm to the extracellular space. Although previous in vitro experiments have demonstrated highly specific interactions between CusF and CusB that are crucial for metal transfer to occur, the structural details of the interaction have not been determined. Here, the interactions between CusF and CusB are mapped through nuclear magnetic resonance (NMR) spectroscopy and chemical cross-linking coupled with high-resolution mass spectrometry to better understand how recognition and metal transfer occur between these proteins. The NMR (1)H-(15)N correlation spectra reveal that CusB interacts with the metal-binding face of CusF. In vitro chemical cross-linking with a 7.7 Å homobifunctional amine-reactive cross-linker, BS(2)G, was used to capture the CusF/CusB interaction site, and mass spectral data acquired on an LTQ-Orbitrap confirm the following two cross-links: CusF K31 to CusB K29 and CusF K58 to CusB K32, thus revealing that the N-terminal region of CusB interacts with the metal-binding face of CusF. The proteins transiently interact in a metal-dependent fashion, and contacts between CusF and CusB are localized to regions near their respective metal-binding sites.
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