Claudine Darnault

ORCID: 0000-0001-7777-2381
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About
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Research Areas
  • Metalloenzymes and iron-sulfur proteins
  • Enzyme Structure and Function
  • Hydrogen Storage and Materials
  • Immune Cell Function and Interaction
  • T-cell and B-cell Immunology
  • Biochemical and Molecular Research
  • Bacteriophages and microbial interactions
  • CAR-T cell therapy research
  • Phagocytosis and Immune Regulation
  • Photosynthetic Processes and Mechanisms
  • Bacterial Genetics and Biotechnology
  • Advanced Fluorescence Microscopy Techniques
  • Electrocatalysts for Energy Conversion
  • Biofuel production and bioconversion
  • Microbial Metabolic Engineering and Bioproduction
  • Cell death mechanisms and regulation
  • Complement system in diseases
  • Immunotherapy and Immune Responses
  • Trace Elements in Health
  • Metal-Catalyzed Oxygenation Mechanisms
  • Iron Metabolism and Disorders
  • Graphene research and applications
  • Erythrocyte Function and Pathophysiology
  • Hemoglobin structure and function
  • Galectins and Cancer Biology

Institut de Biologie Structurale
2012-2024

CEA Grenoble
2003-2022

Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2005-2022

Centre National de la Recherche Scientifique
2006-2022

Université Grenoble Alpes
2002-2022

Université Joseph Fourier
2000-2012

Institut Pasteur
2002

C1q is a versatile recognition protein that binds to an amazing variety of immune and non-immune ligands triggers activation the classical pathway complement. The crystal structure globular domain responsible for its properties has now been solved refined 1.9 Å resolution. reveals compact, almost spherical heterotrimeric assembly held together mainly by non-polar interactions, with Ca2+ ion bound at top. appears be key factor this protein. Plausible three-dimensional models in complex two...

10.1074/jbc.m307764200 article EN cc-by Journal of Biological Chemistry 2003-11-01

Abstract Efficient apoptotic cell clearance is critical for maintenance of tissue homeostasis, and to control the immune responses mediated by phagocytes. Little known about molecules that contribute “eat me” signals on surface. C1q, recognition unit C1 complex complement, also senses altered structures from self a major actor tolerance. HeLa cells were rendered UV-B treatment variety cellular molecular approaches used investigate nature target(s) recognized C1q. Using surface plasmon...

10.4049/jimmunol.180.4.2329 article EN The Journal of Immunology 2008-02-15

The crystal structure of the membrane-bound O 2 -tolerant [NiFe]-hydrogenase 1 from Escherichia coli ( Ec Hyd-1) has been solved in three different states: as-isolated, H -reduced, and chemically oxidized. As very recently reported for similar enzymes Ralstonia eutropha Hydrogenovibrio marinus , two supernumerary Cys residues coordinate proximal [FeS] cluster Hyd-1, which lacks one inorganic sulfide ligands. We find that aerobically purified species contains a mixture at least conformations...

10.1073/pnas.1119806109 article EN Proceedings of the National Academy of Sciences 2012-03-19

Most bacteriophages present a tail allowing host recognition, cell wall perforation, and viral DNA channeling from the capsid to infected bacterium cytoplasm. The majority of tailed phages bear long flexible ( Siphoviridae ) at tip which receptor binding proteins (RBPs) specifically interact with their host, triggering infection. In siphophage T5, unique RBP is located extremity central fiber. We structures T5 tip, determined by cryo–electron microscopy before after interaction its E. coli...

10.1126/sciadv.ade9674 article EN cc-by-nc Science Advances 2023-03-24

Abstract NsrR from Streptomyces coelicolor ( Sc) regulates the expression of three genes through progressive degradation its [4Fe–4S] cluster on nitric oxide (NO) exposure. We report 1.95 Å resolution crystal structure dimeric holo-ScNsrR and show that is coordinated by invariant Cys residues one monomer and, unexpectedly, Asp8 other. A cavity map suggests NO displaces as a ligand while D8A D8C variants remain sensitive, DNA binding affected. structural comparison with an apo-IscR-DNA...

10.1038/ncomms15052 article EN cc-by Nature Communications 2017-04-20

We have observed the photoactivatable fluorescent protein IrisFP in a transient dark state with near-atomic resolution. This is assigned to radical species that either relaxes ground or evolves into permanently bleached chromophore. took advantage of X-rays populate radical, which presumably forms under illumination visible light by an electron-transfer reaction triplet state. The combined X-ray diffraction and crystallo UV−vis absorption, fluorescence, Raman data reveal formation involves...

10.1021/ja907296v article EN Journal of the American Chemical Society 2009-12-01

The dimerization of the O 2 sensor FNR is regulated by extremely fine-tuned interactions.

10.1126/sciadv.1501086 article EN cc-by-nc Science Advances 2015-12-04

The recently discovered Rrf2 family transcriptional regulator RsrR coordinates a [2Fe–2S] cluster. Remarkably, binding of the protein to RsrR-regulated promoter DNA sequences is switched on and off through facile cycling cluster between +2 +1 states. Here, we report high resolution crystal structures dimer, revealing that asymmetrically coordinated across monomer–monomer interface by two Cys residues from one subunit His Glu other. To our knowledge, this first example bound [Fe–S] with three...

10.1021/jacs.8b10823 article EN cc-by Journal of the American Chemical Society 2019-01-18

Quinolinate synthase (NadA) is a Fe4S4 cluster-containing dehydrating enzyme involved in the synthesis of quinolinic acid (QA), universal precursor essential nicotinamide adenine dinucleotide (NAD) coenzyme. A previously determined apo NadA crystal structure revealed binding one substrate analog, providing partial mechanistic information. Here, we report on holo X-ray NadA. The presence cluster generates an internal tunnel and cavity which have docked last to be dehydrated form QA. We find...

10.1021/ja501431b article EN Journal of the American Chemical Society 2014-03-20

The Escherichia coli fumarate and nitrate reduction (FNR) regulator acts as the cell’s master switch for transition between anaerobic aerobic respiration, controlling expression of >300 genes in response to O2 availability. Oxygen is perceived through a reaction with FNR’s [4Fe-4S] cluster cofactor. In addition its primary signal, FNR also reacts nitric oxide (NO). physiological concentrations NO, de-represses transcription hmp, which encodes principal NO-detoxifying enzyme, fails...

10.3390/inorganics11120450 article EN cc-by Inorganics 2023-11-21

The enzyme NadA catalyzes the synthesis of quinolinic acid (QA), precursor universal nicotinamide adenine dinucleotide (NAD) cofactor. Here, we report crystal structures complexes between Thermotoga maritima (Tm) K219R/Y107F variant and (i) first intermediate (W) resulting from condensation dihydroxyacetone phosphate (DHAP) with iminoaspartate (ii) DHAP analogue triose-phosphate isomerase inhibitor phosphoglycolohydroxamate (PGH). In addition, using TmNadA K219R/Y21F variant, have reacted...

10.1021/jacs.6b05884 article EN Journal of the American Chemical Society 2016-08-22

Ni-dependent acetyl-CoA synthase (ACS) and CO dehydrogenase (CODH) constitute the central enzyme complex of Wood−Ljungdahl pathway formation. The crystal structure a recombinant bacterial ACS lacking N-terminal domain that interacts with CODH shows large reorganization remaining two globular domains, producing narrow cleft suitable size, shape, nature to bind CoA. Sequence comparisons homologous archaeal enzymes naturally lack show many amino acids lining this are conserved. Besides typical...

10.1021/bi9003952 article EN Biochemistry 2009-07-13

NadA is a multifunctional enzyme that condenses dihydroxyacetone phosphate (DHAP) with iminoaspartate (IA) to generate quinolinic acid (QA), the universal precursor of nicotinamide adenine dinucleotide (NAD(P)) cofactor. Using X-ray crystallography, we have (i) characterized two reaction intermediates QA synthesis using "pH-shift" approach and slowly reacting Thermotoga maritima variant (ii) observed product, resulting from degradation an intermediate analogue, bound close entrance long...

10.1021/acschembio.7b01104 article EN ACS Chemical Biology 2018-04-11

A combined experimental and computational study of an O<sub>2</sub>-tolerant [NiFe]-hydrogenase mutated proximal FeS cluster with possible applications to similar problems.

10.1039/c8cc02896f article EN Chemical Communications 2018-01-01

Iron-regulatory proteins (IRPs) 1 and 2 are closely related molecules involved in animal iron metabolism. Both can bind to specific mRNA regions called iron-responsive elements thereby control the expression of uptake, storage utilization iron. In iron-replete cells, IRP1, but not IRP2, binds a [4Fe–4S] cluster functions as cytoplasmic aconitase, with simultaneous loss its RNA-binding ability. Whereas IRP2 is known be Fe homeostasis, role IRP1 less clear; it may provide link between citrate...

10.1107/s1744309105010444 article EN Acta Crystallographica Section F Structural Biology and Crystallization Communications 2005-04-09

Abstract The vast majority of bacteriophages (phages) - bacterial viruses present a tail that allows host recognition, cell wall perforation and safe channelling the viral DNA from capsid to cytoplasm infected bacterium. tailed phages bears long flexible ( Siphoviridae ) at distal end which tip complex, often called baseplate, harbours one or more Receptor Binding Protein·s (RBPs). Interaction between RBPs surface triggers ejection, but little is known on these mechanisms for . Here, we...

10.1101/2022.09.20.507954 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2022-09-20

Quinolinate synthase (NadA) is a [4Fe-4S] cluster-containing enzyme involved in the formation of quinolinic acid, precursor essential NAD coenzyme. Here, we report synthesis and activity derivatives first inhibitor NadA. Using multidisciplinary approaches have investigated their action mechanism discovered additional specific inhibitors this enzyme.

10.1039/c8cc09023h article EN Chemical Communications 2019-01-01
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