ArticleBiochemistry2012
N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Mechanisms of Copper Selectivity and Release by the Metallochaperone CusF: Insights from CO-Binding, Rapid-Freeze-Quench EXAFS, and Unnatural Amino Acid Substitution.Inorganic chemistry · 2024Article
- The copper resistance mechanism in a newly isolated Pseudoxanthomonas spadix ZSY-33.Environmental microbiology reports · 2023Article
- 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
- NMR reveals the interplay between SilE and SilB model peptides in the context of silver resistance.Chemical communications (Cambridge, England) · 2021Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Catalytic M Center of Copper Monooxygenases Probed by Rational Design. Effects of Selenomethionine and Histidine Substitution on Structure and Reactivity.Biochemistry · 2019Article
- Inhibiting the copper efflux system in microbes as a novel approach for developing antibiotics.PloS one · 2019Article
- Exploring the role of the various methionine residues in the Escherichia coli CusB adapter protein.PloS one · 2019Article
- 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
- Kβ Valence to Core X-ray Emission Studies of Cu(I) Binding Proteins with Mixed Methionine - Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase.Inorganic chemistry · 2016Article
- Extracellular Proteins: Novel Key Components of Metal Resistance in Cyanobacteria?Frontiers in microbiology · 2016Article
- AztD, a Periplasmic Zinc Metallochaperone to an ATP-binding Cassette (ABC) Transporter System in Paracoccus denitrificans.The Journal of biological chemistry · 2015Article
- CopM is a novel copper-binding protein involved in copper resistance in Synechocystis sp. PCC 6803.MicrobiologyOpen · 2015Article
- The ins and outs of RND efflux pumps in Escherichia coli.Frontiers in microbiology · 2015Review
- Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies.Frontiers in microbiology · 2015Review
- 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
- Bacterial multidrug efflux transporters.Annual review of biophysics · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Gram-negative bacteria, such as Escherichia coli, utilize efflux resistance systems in order to expel toxins from their cells. Heavy-metal resistance is mediated by resistance nodulation cell division (RND)-based efflux pumps composed of a tripartite complex that includes an RND-transporter, an outer-membrane factor (OMF), and a membrane fusion protein (MFP) that spans the periplasmic space. MFPs are necessary for complex assembly and have been hypothesized to play an active role in substrate efflux. Crystal structures of MFPs are available, however incomplete, as large portions of the apparently disordered N- and C-termini are unresolved. Such is the case for CusB, the MFP of the E. coli Cu(I)/Ag(I) efflux pump CusCFBA. In this work, we have investigated the structure and function of the N-terminal region of CusB, which includes the metal-binding site and is missing from previously determined crystal structures. Results from mass spectrometry and X-ray absorption spectroscopy show that the isolated N-terminal 61 residues (CusB-NT) bind metal in a 1:1 stoichiometry with a coordination site composed of M21, M36, and M38, consistent with full-length CusB. NMR spectra show that CusB-NT is mostly disordered in the apo state; however, some slight structure is adopted upon metal binding. Much of the intact protein's function is maintained in this fragment as CusB-NT binds metal in vivo and in vitro, and metal is transferred between the metallochaperone CusF and CusB-NT in vitro. Functional analysis in vivo shows that full-length CusB is necessary in an intact polypeptide for full metal resistance, though CusB-NT alone can contribute partial metal resistance. These findings reinforce the theory that the role of CusB is not only to bind metal but also to play an active role in efflux.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.