Ribosomes & Translation Regulation; Antibiotics & Resistance Mechanisms; Structural Biology & Cryo-EM; University of Hamburg.
Wilson Lab
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Nature research paper: A natural depsipeptide antibiotic binds the E-site of the bacterial ribosome
go.nature.com/3RMNwPW
journals.iucr.org/m/issues/202...
Kurianlab
Nature
www.nature.com/articles/s41...
#microsky
🧪🦠 Streptomyces rimosus
"Das Antibiotikum mit dem Namen Manikomycin wirkt gegen multiresistente Bakterien und könnte langfristig zur Entwicklung neuer Behandlungsoptionen beitragen"
www.welt.de/gesundheit/a...
👇
www.nature.com/articles/s41...
www.genengnews.com/topics/infec...
🚨 New in @natureportfolio.nature.com! 🚨
Excited to share our discovery of Manikomycin—a novel antibiotic tackling the AMR crisis! 🦠
Using cryo-EM, we found it’s the first-in-class to target the ribosomal E-site, blocking tRNA entry and beating multi-drug resistance.
Read: doi.org/10.1038/s415...
The latest from the lab. Manikomycin, a new cyclic depsipeptide antibiotic from an 'old' source, the oxytetracycline producer Streptomyces rimosus. Still lots to be learned from this genus! Manikomycin blocks the E-site of the bacterial ribosome. A first.
links.springernature.com/f/a/Q0JMeeZK...
Our new smFRET assay to follow intersubunit rotation of eukaryotic ribosomes during translation elongation is out:
academic.oup.com/nar/article/...
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of the bacterial large ribosomal subunit.
go.nature.com
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of ...
Abstract. Translation is accompanied by the rotation of the small and large ribosomal subunits relative to each other. Here, we use single-molecule Förster
🚨 New in @natcomms.nature.com 🚨
Excited to share our paper on how proline-rich antimicrobial peptides interact with the bacterial ribosome.
Using cryo-EM, we found that tiny sequence changes cause these peptides to "flip" orientation in the exit tunnel! 🔄🧫
Read: www.nature.com/articles/s41...
New paper in @natcomms.nature.com! We show how the Clostridia peptide CliM acts as a molecular handbrake to monitor YidC activity.
Cryo-EM & MD show it stalls the ribosome using diverse mechanisms until membrane insertion releases it.
Paper: www.nature.com/articles/s41...
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of ...
Researchers discover manikomycin, a novel antibiotic that kills drug-resistant bacteria by targeting a previously unknown ribosomal target.
www.genengnews.com
Gorgias UrUrUrenkel📣🔊
www.nature.com
In this work authors show how minimal mutations in proline-rich antimicrobial peptides can flip their orientation in the ribosome exit tunnel, switching their mechanism from stalling translation termi...
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of ...
Ausgerechnet ein lange erforschter Mikroorganismus liefert einen bislang unbekannten Wirkstoff gegen multiresistente Keime. Manikomycin ist noch weit von der Klinik entfernt – zeigt aber, wo die Antib...
www.welt.de
Haaris Ahsan Safdari
Haaris Ahsan Safdari
CliM is a ribosome arrest peptide in Clostridia. Here, the authors show that CliM adopts helices and extensively interacts with the ribosome. The penultimate residue sterically blocks A-site accommoda...
