ArticleBiochemistry2018
Crystal Structure of the Siderophore Binding Protein BauB Bound to an Unusual 2:1 Complex Between Acinetobactin and Ferric Iron.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Arylthiazoline Unit as a Ferric Ion Chelating Moiety in Siderophores: The Coordination Chemistry of Anguibactin and Its Analogs.Inorganic chemistry · 2026Article
- Exploring Metalloproteome Remodeling in Calprotectin-StressedACS chemical biology · 2025Article
- Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025Article
- Article
- Bioinformatics and modelling studies of FhuD, the periplasmic siderophore binding protein from the plant pathogen Erwinia amylovora.PloS one · 2025Article
- Location, Location, Location: Establishing Design Principles for New Antibacterials from Ferric Siderophore Transport Systems.Molecules (Basel, Switzerland) · 2024Review
- Synthesis and Characterization of Preacinetobactin and 5-Phenyl Preacinetobactin.Molecules (Basel, Switzerland) · 2022Article
- Article
- Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein fromACS omega · 2021Article
- Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics.Chemical reviews · 2021Review
- Comparative genome analyses ofMicrobial genomics · 2020Article
- Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020Review
- Carbapenemases: TransformingBiomolecules · 2020Review
- Emergence of Ferrichelatase Activity in a Siderophore-Binding Protein Supports an Iron Shuttle in Bacteria.ACS central science · 2020Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The critical role that iron plays in many biochemical processes has led to an elaborate battle between bacterial pathogens and their hosts to acquire and withhold this critical nutrient. Exploitation of iron nutritional immunity is being increasingly appreciated as a potential antivirulence therapeutic strategy, especially against problematic multidrug resistant Gram-negative pathogens such as Acinetobacter baumannii. To facilitate iron uptake and promote growth, A. baumannii produces a nonribosomally synthesized peptide siderophore called acinetobactin. Acinetobactin is unusual in that it is first biosynthesized in an oxazoline form called preacinetobactin that spontaneously isomerizes to the final isoxazolidinone acinetobactin. Interestingly, both isomers can bind iron and both support growth of A. baumannii. To address how the two isomers chelate their ferric cargo and how the complexes are used by A. baumannii, structural studies were carried out with the ferric acinetobactin complex and its periplasmic siderophore binding protein BauB. Herein, we present the crystal structure of BauB bound to a bis-tridentate (Fe
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