A5062679890- Bacterial Genetics and Biotechnology
- RNA and protein synthesis mechanisms
- Bacteriophages and microbial interactions
- Enzyme Structure and Function
- CRISPR and Genetic Engineering
- Genomics and Phylogenetic Studies
- NMR spectroscopy and applications
- Peptidase Inhibition and Analysis
- Advanced NMR Techniques and Applications
- Carbohydrate Chemistry and Synthesis
- Protein Structure and Dynamics
- Streptococcal Infections and Treatments
- Antibiotic Resistance in Bacteria
- Machine Learning in Bioinformatics
- Enzyme Production and Characterization
- Chemical Synthesis and Analysis
- Toxin Mechanisms and Immunotoxins
- Pneumonia and Respiratory Infections
- Lipid metabolism and disorders
- Hippo pathway signaling and YAP/TAZ
- Microbial Natural Products and Biosynthesis
- Bacterial Infections and Vaccines
- ATP Synthase and ATPases Research
MRC Laboratory of Molecular Biology
2019-2023
Medical Research Council
2020-2023
Institut de Biologie Structurale
2014-2016
Université Grenoble Alpes
2014-2016
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2014
CEA Grenoble
2014
Centre National de la Recherche Scientifique
2014
Significance Bacteria surround their cytoplasmic membrane with an essential heteropolymer, the peptidoglycan (PG) sacculus, to maintain osmotic stability and cell shape. Cells enlarge sacculus by using membrane-anchored PG synthases, which are guided cytoskeletal elements. Gram-negative bacteria have a thin, mainly single-layered connected outer membrane. Outer-membrane–anchored lipoproteins were recently found be for growth. Here, we present structure of protein LpoB Escherichia coli , is...
Highlights•LpoA's N-terminal domain features an all-α-helical fold similar to TPR domains•The C-terminal of E. coli LpoA contains two extensive flexible regions•Full-length adopts elongated structure with low interdomain flexibility•LpoA can span the periplasm stimulate peptidoglycan synthase PBP1ASummaryThe bacterial cell envelope stress-bearing layer, which is enlarged during growth and division by membrane-anchored synthases guided cytoskeletal elements. In Escherichia coli, major PBP1A...
FtsK protein contains a fast DNA motor that is involved in bacterial chromosome dimer resolution. During cell division, translocates double-stranded until both dif recombination sites are placed at mid for subsequent Here, we solved the 3.6-Å resolution electron cryo-microscopy structure of domain while translocating on its substrate. Each subunit homo-hexameric ring adopts unique conformation and one three nucleotide states. Two DNA-binding loops within four subunits form pair spiral...
Abstract Accurate placement of the bacterial division site is a prerequisite for generation two viable and identical daughter cells. In Streptococcus pneumoniae , positive regulatory mechanism involving membrane protein MapZ positions precisely conserved cell FtsZ at centre. Here we characterize structure extracellular domain show that it displays bi-modular composed subdomains separated by flexible serine-rich linker. We further demonstrate in vivo N-terminal subdomain serves as pedestal...
Bacteria surround their cytoplasmic membrane with the essential heteropolymer peptidoglycan (PG), which is made of glycan chains cross-linked by short peptides, to maintain osmotic stability and cell shape. PG assembled from lipid II precursor glycosyltransferase transpeptidase reactions catalyzed synthases, are anchored controlled inside cytoskeletal elements. Recently, two lipoproteins, LpoA LpoB, were shown be required in Escherichia coli for activating main Penicillin-Binding Proteins 1A...
Cell division, or cytokinesis is a fundamental process of life and, in most bacteria, driven by peptidoglycan synthesis at the septum 1 . It catalysed divisome, multi-protein complex with more than 20 components that spans cell envelope bacteria harbouring wall 2 Central to divisome peptidoglycan-synthesising protein FtsWI, transglycosylase (TG) FtsW polymerising glycan strands from its substrate Lipid II 3,4 , and transpeptidase (TP) FtsI crosslinking peptide stems, thus forming covalent...
Abstract FtsK protein contains a fast DNA motor involved in bacterial chromosome dimer resolution. To understand how moves DNA, we solved the 3.6 Å resolution cryo-EM structure of domain while translocating double-stranded DNA. Each subunit hexameric ring adopts unique conformation and one three nucleotide states. Two DNA-binding loops within four subunits form pair spiral staircases ring, interacting with two strands. This suggests that simultaneous conformational changes all ATPase domains...