ArticleThe EMBO journal1993
Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli.
Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 133 citations in OpenAlex.
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- Does the lipid environment impact the open-state conductance of an engineered β-barrel protein nanopore?Biochimica et biophysica acta · 2013Article
- TonB-dependent transporter FhuA in planar lipid bilayers: partial exit of its plug from the barrel.Biochemistry · 2012Article
- Evidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transport.Metallomics : integrated biometal science · 2012Article
- First insights on organic cosolvent effects on FhuA wildtype and FhuA Δ1-159.International journal of molecular sciences · 2012Article
- Redesign of a plugged beta-barrel membrane protein.The Journal of biological chemistry · 2011Article
- Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- TonB induces conformational changes in surface-exposed loops of FhuA, outer membrane receptor of Escherichia coli.Protein science : a publication of the Protein Society · 2008Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Deletion variants of Neurospora mitochondrial porin: electrophysiological and spectroscopic analysis.Biophysical journal · 2006Article
- ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus.Journal of bacteriology · 2005Article
- Defined inactive FecA derivatives mutated in functional domains of the outer membrane transport and signaling protein of Escherichia coli K-12.Journal of bacteriology · 2004Article
- Loop deletions indicate regions important for FhuA transport and receptor functions in Escherichia coli.Journal of bacteriology · 2004Article
- In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12.Journal of bacteriology · 2003Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The FhuA receptor protein is involved in energy-coupled transport of Fe3+ via ferrichrome through the outer membrane of Escherichia coli. Since no energy source is known in the outer membrane it is assumed that energy is provided through the action of the TonB, ExbB and ExbD proteins, which are anchored to the cytoplasmic membrane. By deleting 34 amino acid residues of a putative cell surface exposed loop, FhuA was converted from a ligand specific transport protein into a TonB independent and nonspecific diffusion channel. The FhuA deletion derivative FhuA delta 322-355 formed stable channels in black lipid membranes, in contrast to wild-type FhuA which did not increase membrane conductance. The single-channel conductance of the FhuA mutant channels was at least three times larger than that of the general diffusion porins of E. coli outer membrane. It is proposed that the basic structure of FhuA in the outer membrane is a channel formed by beta-barrels. Since the loop extending from residue 316 to 356 is part of the active site of FhuA, it probably controls the permeability of the channel. The transport-active conformation of FhuA is mediated by a TonB-induced conformational change in response to the energized cytoplasmic membrane. The ferrichrome transport rate into cells expressing FhuA delta 322-355 increased linearly with increasing substrate concentration (from 0.5 to 20 microM), in contrast to FhuA wild-type cells, which displayed saturation at 5 microM. This implies that in wild-type cells ferrichrome transport through the outer membrane is the rate-limiting step and that TonB, ExbB and ExbD are only required for outer membrane transport.
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