Search Results - "Talfournier, F."

Unraveling the function of paralogs of the aldehyde dehydrogenase super family from Sulfolobus solfataricus by Esser, D., Kouril, T., Talfournier, F., Polkowska, J., Schrader, T., Bräsen, C., Siebers, B.

“…Aldehyde dehydrogenases (ALDHs) have been well established in all three domains of life and were shown to play essential roles, e.g., in intermediary…”
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A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli by Boschi-Muller, S, Azza, S, Sanglier-Cianferani, S, Talfournier, F, Van Dorsselear, A, Branlant, G

“…Methionine oxidation into methionine sulfoxide is known to be involved in many pathologies and to exert regulatory effects on proteins. This oxidation can be…”
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The First Crystal Structure of a Thioacylenzyme Intermediate in the ALDH Family:  New Coenzyme Conformation and Relevance to Catalysis by D'Ambrosio, Katia, Pailot, Arnaud, Talfournier, François, Didierjean, Claude, Benedetti, Ettore, Aubry, André, Branlant, Guy, Corbier, Catherine

“…Crystal structures of several members of the nonphosphorylating CoA-independent aldehyde dehydrogenase (ALDH) family have shown that the peculiar binding mode…”
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The crystal structure of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP + at 2.1 Å resolution by Charron, C, Talfournier, F, Isupov, M.N, Littlechild, J.A, Branlant, G, Vitoux, B, Aubry, A

“…The crystal structure of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaeon Methanothermus fervidus has been solved in the holo form at 2.1…”
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Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase from Escherichia coli by Tête-Favier, Frédérique, Cobessi, David, Leonard, Gordon A., Azza, Saïd, Talfournier, François, Boschi-Muller, Sandrine, Branlant, Guy, Aubry, André

“…Peptide methionine sulfoxide reductase mediates the reduction of protein sulfoxide methionyl residues back to methionines and could thus be implicated in the…”
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Extensive conformational sampling in a ternary electron transfer complex by Leys, David, Basran, Jaswir, Talfournier, François, Sutcliffe, Michael J, Scrutton, Nigel S

“…Here we report the crystal structures of a ternary electron transfer complex showing extensive motion at the protein interface. This physiological complex…”
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Crystallization and preliminary X-ray diffraction studies of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus by Charron, C., Talfournier, F., Isupov, M. N., Branlant, G., Littlechild, J. A., Vitoux, B., Aubry, A.

“…The homotetrameric holo‐d‐glyceraldehyde‐3‐phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus has been crystallized in the…”
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Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis by Stines-Chaumeil, Claire, Talfournier, François, Branlant, Guy

“…Homotetrameric MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis catalyses the NAD-dependent oxidation of MMSA (methylmalonate…”
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Invariant Thr super(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans by Pailot, A, D'Ambrosio, K, Corbier, C, Talfournier, F, Branlant, G

“…One of the most striking features of several X-ray structures of CoA-independent ALDHs (aldehyde dehydrogenases) in complex with NAD(P) is the conformational…”
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Invariant Thr244 is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans by Pailot, Arnaud, D'Ambrosio, Katia, Corbier, Catherine, Talfournier, François, Branlant, Guy

“…One of the most striking features of several X-ray structures of CoA-independent ALDHs (aldehyde dehydrogenases) in complex with NAD(P) is the conformational…”
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Expression, purification, crystallization and preliminary X-ray diffraction data of methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis by Dubourg, Hélène, Stines-Chaumeil, Claire, Didierjean, Claude, Talfournier, François, Rahuel-Clermont, Sophie, Branlant, Guy, Aubry, André

“…Methylmalonate‐semialdehyde dehydrogenase from Bacillus subtilis was cloned and overexpressed in Escherichia coli. Suitable crystals for X‐ray diffraction…”
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Electron Transfer and Conformational Change in Complexes of Trimethylamine Dehydrogenase and Electron Transferring Flavoprotein by Jones, Matthew, Talfournier, Francois, Bobrov, Anton, Grossmann, J. Günter, Vekshin, Nikolai, Sutcliffe, Michael J., Scrutton, Nigel S.

“…The trimethylamine dehydrogenase-electron transferring flavoprotein (TMADH·ETF) electron transfer complex has been studied by fluorescence and absorption…”
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alpha Arg-237 in Methylophilus methylotrophus (sp. W sub(3)A sub(1)) Electron-transferring Flavoprotein Affords similar to 200-Millivolt Stabilization of the FAD Anionic Semiquinone and a Kinetic Block on Full Reduction to the Dihydroquinone by Talfournier, F, Munro, A W, Basran, J, Sutcliffe, MJ, Daff, S, Chapman, S K, Scrutton, N S

“…The midpoint reduction potentials of the FAD cofactor in wild-type Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein (ETF) and the…”
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alpha Arg-237 in Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein affords approximately 200-millivolt stabilization of the FAD anionic semiquinone and a kinetic block on full reduction to the dihydroquinone by Talfournier, F, Munro, A W, Basran, J, Sutcliffe, M J, Daff, S, Chapman, S K, Scrutton, N S

“…The midpoint reduction potentials of the FAD cofactor in wild-type Methylophilus methylotrophus (sp. W3A1) electron-transferring flavoprotein (ETF) and the…”
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The Crystal Structure of Glyceraldehyde-3-phosphate Dehydrogenase from the Hyperthermophilic Archaeon Methanothermus fervidus in the Presence of NADP at 2.1 Aa Resolution by Charron, C, Talfournier, F, Isupov, M, Littlechild, J, Branlant, G, Vitoux, B, Aubry, A

“…The crystal structure of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaeon Methanothermus fervidus has been solved in the holo form at 2.1…”
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Comparative study of the catalytic domain of phosphorylating glyceraldehyde‐3‐phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site‐directed mutagenesis by Talfournier, François, Colloc'h, Nathalie, Mornon, Jean‐Paul, Branlant, Guy

“…Phosphorylating glyceraldehyde‐3‐phosphate dehydrogenase (GraP‐DH) catalyzes the oxidative phosphorylation of D‐glyceraldehyde‐3‐phosphate to form…”
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Flavin radicals, conformational sampling and robust design principles in interprotein electron transfer: the trimethylamine dehydrogenase-electron-transferring flavoprotein complex by Leys, David, Basran, Jaswir, Talfournier, François, Chohan, Kamaldeep K, Munro, Andrew W, Sutcliffe, Michael J, Scrutton, Nigel S

“…TMADH (trimethylamine dehydrogenase) is a complex iron-sulphur flavoprotein that forms a soluble electron-transfer complex with ETF (electron-transferring…”
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Thermal unfolding of phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry by Levashov, Pavel, Orlov, Victor, Boschi-Muller, Sandrine, Talfournier, Francois, Asryants, Regina, Bulatnikov, Igor, Muronetz, Vladimir, Branlant, Guy, Nagradova, Natalya

“…Thermal unfolding parameters were determined for a two-domain tetrameric enzyme, phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and for…”
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Functional characterization of the phosphorylating D‐glyceraldehyde 3‐phosphate dehydrogenase from the archaeon Methanothermus fervidus by comparative molecular modelling and site‐directed mutagenesis by Talfournier, François, Colloc’h, Nathalie, Mornon, Jean‐Paul, Branlant, Guy

“…Phosphorylating archaeal d‐glyceraldehyde 3‐phosphate dehydrogenases (GraP‐DHs) share only 15–20% identity with their glycolytic bacterial and eukaryotic…”
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