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Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate Inra
Ferrer, J.L.; Ravanel, S.; Robert, M.; Dumas, R..
Cobalamin-independent methionine synthase (MetE) catalyzes the synthesis of methionine by a direct transfer of the methyl group of N5-methyltetrahydrofolate (CH3-H4PteGlun) to the sulfur atom of homocysteine (Hcy). We report here the first crystal structure of this metalloenzyme under different forms, free or complexed with the Hcy and folate substrates. The Arabidopsis thaliana MetE (AtMetE) crystals reveal a monomeric structure built by two (βα)8 barrels making a deep groove at their interface. The active site is located at the surface of the C-terminal domain, facing the large interdomain cleft. Inside the active site, His647, Cys649, and Cys733 are involved in zinc coordination, whereas Asp605, Ile437, and Ser439 interact with Hcy. Opposite the...
Tipo: Journal Article Palavras-chave: ARABIDOPSIS THALIANA; STRUCTURE TRIDIMENSIONNELLE; SITE ACTIF; HOMOCYSTEINE; FOLATE; SITE DE LIAISON; ZINC; METHIONINE.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0500031912109810&uri=/notices/prodinra1/2010/11/
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Enzyme-induced covalent modification of methionyl-tRNA synthetase from Bacillus stearothermophilus by methionyl-adenylate : identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry Inra
Hountondji, C.; Beauvallet, C.; Pernollet, J.C.; Blanquet, S..
Methionyl-tRNA synthetase (MetRS) from Bacillus stearothermophilus was shown to undergo covalent methionylation by a donor methionyl-adenylate, the mixed carboxylic-phosphoric acid anhydride synthesized by the enzyme itself. Covalent reaction of methionyl-adenylate with the synthetase or other proteins proceeds through the formation of an isopeptide bond between the carboxylate of the amino acid and the ε-NH2 group of lysyl residues. The stoichiometries of labeling, as followed by TCA precipitation, were 2.2 ± 0.1 and 4.3 ± 0.1 mol of [14C]Met incorporated by 1 mol of the monomeric MS534 and the native dimeric species of B. stearo methionyl-tRNA synthetase, respectively. Matrix-assisted laser desorption-ionization mass spectrometry designated lysines-261,...
Tipo: Journal Article Palavras-chave: SYNTHETASE D'ARN DE TRANSFERT; METHIONINE; EXTREMITE 3'; ADENYLATE METHIONYLE; LIEN ISOPEPTIDE; MALDI-MS; MODIFICATION POSTTRANSLATIONNELLE; SITE DE LIAISON; ORDRE DE SIGNATURE; LEVURE DE BOULANGER; ACTIVATION; MECANISME METHIONYL-tRNA SYNTHETASE; METHIONYL-ADENYLATE; ISOPEPTIDE BOND; MALDI-MS; POSTTRANSLATIONAL MODIFICATION.
Ano: 2000 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0600023845111614&uri=/notices/prodinra1/2010/12/
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NMR molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction Inra
Casset, F.; Hamelryck, T.; Loris, R.; Brisson, J.R.; Tellier, C.; Dao-Thi, M.H.; Wyns, L.; Poortmans, F.; Perez, S.; Imberty, A..
Tipo: Journal Article Palavras-chave: MODELISATION MOLECULAIRE; SITE DE LIAISON; INTERACTION GLUCIDE PROTEINE; LECTINE; SACCHAROSE; SPECTROMETRIE RMN; CRISTALLOGRAPHIE.
Ano: 1995 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB9500012652052759&uri=/notices/prodinra1/2010/09/
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Tyrosine 105 and threonine 212 at outermost substrate binding subsites –6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1 Inra
Bak-Jensen, K.S.; André, G.; Gottschalk, T.E.; Paës, G.; Tran, V.; Svensson, B..
The role in activity of outer regions in the substrate binding cleft in α-amylases is illustrated by mutational analysis of Tyr105 and Thr212 localized at subsites –6 and +4 (substrate cleavage occurs between subsites –1 and +1) in barley α-amylase 1 (AMY1). Tyr105 is conserved in plant α-amylases whereas Thr212 varies in these and related enzymes. Compared with wild-type AMY1, the subsite –6 mutant Y105A has 140, 15, and <1% activity (kcat/Km) on starch, amylose DP17, and 2-chloro-4-nitrophenyl β-d-maltoheptaoside, whereas T212Y at subsite +4 has 32, 370, and 90% activity, respectively. Thus engineering of aromatic stacking interactions at the ends of the 10-subsite long binding cleft affects activity very differently, dependent on the substrate. Y105A...
Tipo: Journal Article Palavras-chave: LIAISON ENZYME SUBSTRAT; ARRIMAGE; SITE DE LIAISON; MODÉLISATION MOLÉCULAIRE.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0600012057111406&uri=/notices/prodinra1/2010/11/
Registros recuperados: 4
Primeira ... 1 ... Última
 

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