Thierry Izoré

ORCID: 0000-0003-0082-0992
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About
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Research Areas
  • Biochemical and Structural Characterization
  • Bacterial Genetics and Biotechnology
  • Microbial Natural Products and Biosynthesis
  • Bacteriophages and microbial interactions
  • Chemical Synthesis and Analysis
  • Bacterial biofilms and quorum sensing
  • Streptococcal Infections and Treatments
  • Vibrio bacteria research studies
  • RNA and protein synthesis mechanisms
  • Protist diversity and phylogeny
  • Biochemical and Molecular Research
  • Microtubule and mitosis dynamics
  • Genomics and Phylogenetic Studies
  • Antibiotic Resistance in Bacteria
  • Antimicrobial Peptides and Activities
  • Glycosylation and Glycoproteins Research
  • Yersinia bacterium, plague, ectoparasites research
  • Molecular Junctions and Nanostructures
  • Microbial Community Ecology and Physiology
  • ATP Synthase and ATPases Research
  • Phytoplasmas and Hemiptera pathogens
  • Enzyme Structure and Function
  • Pediatric health and respiratory diseases
  • Mass Spectrometry Techniques and Applications
  • Hemoglobin structure and function

Australian Regenerative Medicine Institute
2019-2023

Monash University
2013-2023

EMBL Australia
2018-2023

Clayton Foundation
2018-2021

MRC Laboratory of Molecular Biology
2013-2020

ARC Centre of Excellence in Advanced Molecular Imaging
2018

Medical Research Council
2014

Institut de Biologie Structurale
2008-2012

Université Grenoble Alpes
2009-2012

Centre National de la Recherche Scientifique
2008-2012

MreB is essential for rod shape in many bacteria. Membrane-associated filaments move around the circumference, helping to insert cell wall radial direction reinforce shape. To understand how oriented motion arises, we altered of Bacillus subtilis. isotropic round cells, and orientation restored when externally imposed. Stationary orient within protoplasts, purified tubulates liposomes vitro, orienting tubes. Together, this demonstrates orients along greatest principal membrane curvature, a...

10.7554/elife.32471 article EN cc-by eLife 2018-02-22

Filaments of all actin-like proteins known to date are assembled from pairs protofilaments that arranged in a parallel fashion, generating polarity. In this study, we show the prokaryotic actin homologue MreB forms adopt an antiparallel arrangement vitro and vivo. We provide atomic view Caulobacter as apparent crystal structures. protofilament doublet is essential for MreB's function cell shape maintenance demonstrate by vivo site-specific cross-linking orientation E. coli. 3D cryo-EM shows...

10.7554/elife.02634 article EN cc-by eLife 2014-05-02

Abstract Non-ribosomal peptide synthetases are important enzymes for the assembly of complex natural products. Within these multi-modular lines, condensation domains perform central function chain assembly, typically by forming a bond between two peptidyl carrier protein (PCP)-bound substrates. In this work, we report structural snapshots domain in with an aminoacyl-PCP acceptor substrate. These structures allow identification mechanism that controls access substrates to active site domains....

10.1038/s41467-021-22623-0 article EN cc-by Nature Communications 2021-05-04

Kistamicin is a divergent member of the glycopeptide antibiotics, structurally complex class important, clinically relevant antibiotics often used as last resort against resistant bacteria. The extensively crosslinked structure these that essential for their activity makes chemical synthesis highly challenging and limits production to bacterial fermentation. contains three crosslinks, including an unusual 15-membered A-O-B ring, despite presence only two Cytochrome P450 Oxy enzymes thought...

10.1038/s41467-019-10384-w article EN cc-by Nature Communications 2019-06-13

The similarity of eukaryotic actin to crenactin, a filament-forming protein from the crenarchaeon Pyrobaculum calidifontis supports theory common origin Crenarchaea and Eukaryotes. Monomeric structures crenactin are similar, although their filament architectures were suggested be different. Here we report that forms bona fide double helical filaments show exceptional F-actin. With cryo-electron microscopy reconstruction solved structure 3.8 Å resolution. When forming filaments, 'hydrophobic...

10.7554/elife.21600 article EN cc-by eLife 2016-11-17

Pili are surface-linked virulence factors that play key roles in infection establishment a variety of pathogenic species. In Gram-positive pathogens, pilus formation requires the action sortases, dedicated transpeptidases covalently associate building blocks. Streptococcus pneumoniae, major human pathogen, all genes required for harbored single pathogenicity islet which encodes three structural proteins (RrgA, RrgB, RrgC) and sortases (SrtC-1, SrtC-2, SrtC-3). RrgB forms backbone...

10.1021/bi901261y article EN Biochemistry 2009-10-07

Pseudomonas ΦKZ-like bacteriophages encode a group of related tubulin/FtsZ-like proteins believed to be essential for the correct centring replicated bacteriophage virions within bacterial host. In this study, we present crystal structures protein TubZ from ΦKZ in both monomeric and protofilament states, revealing that undergoes structural changes required polymerise, forming canonical protofilament. Combining our with previous work, propose polymerisation–depolymerisation cycle subgroup...

10.1016/j.jmb.2013.03.019 article EN cc-by Journal of Molecular Biology 2013-03-22

Polymerising proteins of the actin family are nearly ubiquitous. Crenactins, restricted to Crenarchaea, more closely related than bacterial MreB. Crenactins occur in gene clusters hinting at an unknown, but conserved function. We solved crystal structure crenactin 3.2 Å resolution. The protein crystallises as a continuous right‐handed helix with 8 subunits per complete turn, spanning 419 Å. shows several loops that longer actin, overall, is eukaryotic RMSD 1.6 Crenactin filaments imaged by...

10.1016/j.febslet.2014.01.029 article EN cc-by-nc-nd FEBS Letters 2014-01-28

The protein Ebony from Drosophila melanogaster plays a central role in the regulation of histamine and dopamine various tissues through condensation these amines with β-alanine. is rare example nonribosomal peptide synthetase (NRPS) higher eukaryote contains C-terminal sequence that does not correspond to any previously characterized NRPS domain. We have structurally this domain discovered it adopts aryl-alkylamine- N -acetyl transferase (AANAT) fold, which unprecedented biology. Through...

10.1073/pnas.1811194116 article EN Proceedings of the National Academy of Sciences 2019-01-31

In Gram-negative bacteria, the bacterial cell wall biosynthetic mechanism requires coordinated action of enzymes and structural proteins located in cytoplasm, within membrane, periplasm cell. Its main component, peptidoglycan (PG), is essential for division elongation. Penicillin-binding (PBPs) catalyze last steps PG biosynthesis, namely polymerization glycan chains cross-linking stem peptides, can be either monofunctional or bifunctional. Their with that other cell-wall such as lytic...

10.1089/mdr.2012.0006 article EN Microbial Drug Resistance 2012-03-20

Mycobacteria are major environmental microorganisms and cause many significant diseases, including tuberculosis. make an unusual vitamin-like compound, F 420 , use it to both persist during stress resist antibiotic treatment. Understanding how mycobacteria is important, as this process can be targeted create new drugs combat infections like In study, we show that in a way different from other bacteria. We studied the molecular machinery determining chemical mechanism for identifying novel...

10.1128/msystems.00389-20 article EN mSystems 2020-05-18

Cytochrome P450 enzymes (P450s) are a superfamily of monooxygenases that utilize cysteine thiolate-ligated heme moiety to perform wide range demanding oxidative transformations. Given the power active intermediate formed within P450s during their cycle, it is remarkable these can avoid auto-oxidation and retain axial ligand in deprotonated-and thus highly acidic-thiolate form. While little known about process incorporation folding, there an overwhelming preference for one orientation site....

10.3389/fchem.2022.868240 article EN cc-by Frontiers in Chemistry 2022-04-08

10.1007/978-3-319-53047-5_8 article EN Sub-cellular biochemistry/Subcellular biochemistry 2017-01-01

In nonribosomal peptide synthesis, condensation (C) domains are key catalytic that most commonly link carrier protein bound substrates to form peptides or depsipeptides. While adenylation have been well characterized due their role in the selection of monomers and hence as gate keepers biosynthesis, C-domains subject debate they do not apparent “A-domain like” side chain selectivity for acceptor substrates. To probe specificity C-domains, here we report our biochemical structural...

10.3389/fctls.2023.1184959 article EN cc-by Frontiers in Catalysis 2023-06-16

Abstract MreB is essential for rod shape in many bacteria. Membrane-associated filaments move around the circumference, helping to insert cell wall radial direction reinforce shape. To understand how oriented motion arises, we altered of Bacillus subtilis. isotropic round cells, and orientation restored when externally imposed. Stationary orient within protoplasts, purified tubulates liposomes vitro, orienting tubes. Together, this demonstrates orients along greatest principal membrane...

10.1101/197475 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2017-10-02
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