Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides.
Indran Mathavan,Séverine Zirah,Shahid Mehmood,Hassanul G. Choudhury,Christophe Goulard,Yanyan Li,Carol V. Robinson,Sylvie Rebuffat,Konstantinos Beis +8 more
TLDR
The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization and the first structural evidence on the recognition mechanism is provided and biochemical data show that another closely related lasso Peptide cannot interact with F HuA.Abstract:
The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide what is to our knowledge the first structural evidence on the recognition mechanism, and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work provides an explanation on the narrow activity spectrum of lasso peptides and opens the path to the development of new antibacterials.read more
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Iterative model-building, structure refinement, and density modification with the PHENIX AutoBuild Wizard
TL;DR: The highly automated PHENIX AutoBuild wizard is described, which can be applied equally well to phases derived from isomorphous/anomalous and molecular-replacement methods.
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Bacteriocins of lactic acid bacteria: extending the family
TL;DR: This review focuses on the various types of bacteriocins that can be found in LAB and the organization and regulation of the gene clusters responsible for their production and biosynthesis, and considers the food applications of the prototype bacteriOCins from LAB.
Journal ArticleDOI
Beyond iron: non-classical biological functions of bacterial siderophores
TL;DR: An exposition of past and current work into non-classical functions of siderophores is presented and the directions in which this research is headed are highlighted.
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Lasso Peptides: An Intriguing Class of Bacterial Natural Products
TL;DR: The newest findings about the lasso peptides, an emerging class of ribosomally assembled and post-translationally modified peptides from bacteria that were first described in 1991 are discussed and the general methodology to elucidate these structures by NMR will be discussed and pitfalls for these approaches are highlighted.
References
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TL;DR: A description is given of Phaser-2.1: software for phasing macromolecular crystal structures by molecular replacement and single-wavelength anomalous dispersion phasing.
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Scaling and assessment of data quality
TL;DR: The various physical factors affecting measured diffraction intensities are discussed, as are the scaling models which may be used to put the data on a consistent scale and algorithms used by the CCP4 scaling program SCALA.
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Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7.
TL;DR: ARP/wARP 7.0 tackles several tasks: iterative protein model building including a high-level decision-making control module; fast construction of the secondary structure of a protein; building flexible loops in alternate conformations; fully automated placement of ligands; and finding ordered water molecules.
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Bacteriocins — a viable alternative to antibiotics?
TL;DR: Although the application of specific bacteriocins might be curtailed by the development of resistance, an understanding of the mechanisms by which such resistance could emerge will enable researchers to develop strategies to minimize this potential problem.
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