ArticleProtein science : a publication of the Protein Society1998
An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 48 citations in OpenAlex.
- The Thermodynamic Stability of Membrane Proteins in Micelles and Lipid Bilayers Investigated with the Ferrichrom Receptor FhuA.The Journal of membrane biology · 2022Article
- Article
- Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides.Nature chemical biology · 2014Article
- Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its Escherichia coli receptor FhuA.The Journal of biological chemistry · 2013Article
- Small angle neutron scattering for the study of solubilised membrane proteins.The European physical journal. E, Soft matter · 2013Review
- TonB-dependent transporters: regulation, structure, and function.Annual review of microbiology · 2010Review
- Expression, purification, crystallization and preliminary X-ray diffraction analysis of the TonB-dependent haem outer membrane transporter ShuA from Shigella dysenteriae.Acta crystallographica. Section F, Structural biology and crystallization communications · 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
- Pyoverdine-mediated iron uptake in Pseudomonas aeruginosa: the Tat system is required for PvdN but not for FpvA transport.Journal of bacteriology · 2006Article
- Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli.Protein science : a publication of the Protein Society · 2005Article
- Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA.Protein science : a publication of the Protein Society · 2000Article
- Prediction by a neural network of outer membrane beta-strand protein topology.Protein science : a publication of the Protein Society · 1998Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FhuA (Mr 78,992, 714 amino acids), siderophore receptor for ferrichrome-iron in the outer membrane of Escherichia coli, was affinity tagged, rapidly purified, and crystallized. To obtain FhuA in quantities sufficient for crystallization, a hexahistidine tag was genetically inserted into the fhuA gene after amino acid 405, which resides in a known surface-exposed loop. Recombinant FhuA405.H6 was overexpressed in an E. coli strain that is devoid of several major porins and using metal-chelate chromatography was purified in large amounts to homogeneity. FhuA crystals were grown using the hanging drop vapor diffusion technique and were suitable for X-ray diffraction analysis. On a rotating anode X-ray source, diffraction was observed to 3.0 A resolution. The crystals belong to space group P6(1) or P6(5) with unit cell dimensions of a=b=174 A, c=88 A (alpha=beta=90 degrees, gamma=120 degrees).
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