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Amylosucrase, a glucan-synthesizing enzyme from the α-amylase family Inra
Skov, L.K.; Mirza, O.; Henriksen, A.; Potocki de Montalk, G.; Remaud-Simeon, M.; Sarçabal, P.; Willemot, R.M.; Monsan, P.; Gajhede, M..
Amylosucrase (E.C. 2.4.1.4) is a member of Family 13 of the glycoside hydrolases (the α-amylases), although its biological function is the synthesis of amylose-like polymers from sucrose. The structure of amylosucrase from Neisseria polysaccharea is divided into five domains: an all helical N-terminal domain that is not similar to any known fold, a (β/α)8-barrel A-domain, B- and B′-domains displaying α/β-structure, and a C-terminal eight-stranded β-sheet domain. In contrast to other Family 13 hydrolases that have the active site in the bottom of a large cleft, the active site of amylosucrase is at the bottom of a pocket at the molecular surface. A substrate binding site resembling the amylase 2 subsite is not found in amylosucrase. The site is blocked by a...
Tipo: Journal Article Palavras-chave: AMYLOSUCRASE; BACTERIE NON PATHOGENE; NEISSERIA POLYSACCHAREA; ALPHA AMYLASE; SACCHAROSE; STRUCTURE TRIDIMENSIONNELLE; GLYCOGENE; SEQUENCE NUCLEOTIDIQUE; ACTIVITE ENZYMATIQUE; GLYCOSIDE HYDROLYSE; NEISSERICEAE; BACTERIE GRAM NEGATIF; SUCRE.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400023316102157&uri=/notices/prodinra1/2010/10/
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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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Purification and structural analysis of a soluble human chorionogonadotropin hormone-receptor complex Inra
Rémy, J.J.; Nespoulous, C.; Grosclaude, J.; Grébert, D.; Couture, L.; Pajot, E.; Salesse, R..
Receptors for the luteotropin/human chorionogonadotropin hormone belong to the G-protein-coupled receptor family by their membrane-anchoring domains. They also possess a large extracellular domain (ECD) responsible for most of the hormone-receptor interactions. Structure-function studies identified several contacts between hormone and receptor ECD, but the precise topology of the complex is still unknown because of the lack of suitable heterologous expression means. Receptor ECDs exhibit leucine repeats and have been modelized on the basis of the three-dimensional structure of the porcine ribonuclease inhibitor, the first structurally known leucine-rich repeats protein. Here we report overexpression (up to 20 mg per liter) and purification to homogeneity...
Tipo: Journal Article Palavras-chave: TECHNIQUE ANALYTIQUE; STRUCTURE; SPECTROSCOPIE; HORMONE; COMPLEXE HORMONE RECEPTEUR; LH; GONADOTROPINE; IMMUNOPURIFICATION; STRUCTURE TRIDIMENSIONNELLE; PURIFICATION.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0300012808095525&uri=/notices/prodinra1/2010/10/
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Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein Inra
Pons, J.L.; de Lamotte, F.; Gautier, M.F.; Delsuc, M.A..
The refined structure of a wheat type 2 nonspecific lipid transfer protein (ns-LTP2) liganded withl-α-palmitoylphosphatidylglycerol has been determined by NMR. The 15N-labeled protein was produced in Pichia pastoris. Physicochemical conditions and ligandation were intensively screened to obtain the best NMR spectra quality. This ns-LTP2 is a 67-residue globular protein with a diameter of about 30 Å. The structure is composed of five helices forming a right superhelix. The protein presents an inner cavity, which has been measured at 341 Å3. All of the helices display hydrophobic side chains oriented toward the cavity. The phospholipid is found in this cavity. Its fatty acid chain is completely inserted in the protein, the l-α-palmitoylphosphatidylglycerol...
Tipo: Journal Article Palavras-chave: PROTEINE TRANSFERT DE LIPIDE; BIOCHIMIE STRUCTURALE; SPECTROSCOPIE RMN; TECHNIQUE ANALYTIQUE; PICHIA PASTORIS; STRUCTURE TRIDIMENSIONNELLE; PLANTE; SEQUENCE NUCLEOTIDIQUE; PHOSPHOLIPIDE; LIAISON.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400023062101609&uri=/notices/prodinra1/2010/11/
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Structure of a liganded type 2 wheat non-specific lipid transfer protein and the molecular basis of lipid binding Inra
Hoh, F.; Pons, J.-L.; Gautier, M.F.; De Lamotte, F.; Dumas, C..
In plants, a family of ubiquitous proteins named non-specific lipid-transfer proteins (ns-LTPs) facilitates the transfer of fatty acids, phospholipids and steroids between membranes. Recent data suggest that these secreted proteins play a key role in the formation of cuticular wax layers and in defence mechanisms against pathogens. In this study, X-ray crystallography has been used to examine the structural details of the interaction between a wheat type 2 ns-LTP and a lipid, l-­α-­palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 Å resolution by direct methods. The typical α-­helical bundle fold of this protein is maintained by four disulfide bridges and delineates two hydrophobic cavities. The inner surface of the main...
Tipo: Journal Article Palavras-chave: PROTEINE DE TRANSFERT DES LIPIDES; LPT; STRUCTURE TRIDIMENSIONNELLE; CUTICULE NS-LTP2; LIPID-TRANSFER PROTEIN; LIPID BINDING.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200711dfadf3&uri=/notices/prodinra1/2009/03/
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The insect attractant 1-Octen-3-o1 is the natural ligand of bovine odorant-binding protein Inra
Ramoni, R.; Vincent, F.; Grolli, S.; Conti, V.; Malosse, C.; Boyer, F.D.; Nagnan-Le Meillour, P.; Spinelli, S.; Cambillau, C.; Tegoni, M..
Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-Å resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996)Nat. Struct. Biol. 3, 863–867; Bianchet et al.(1996) Nat. Struct. Biol. 3, 934–939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-Å resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body...
Tipo: Journal Article Palavras-chave: TECHNIQUE ANALYTIQUE; SPECTROMÉTRIE DE MASSE; CHROMATOGRAPHIE EN PHASE GAZEUSE; STRUCTURE TRIDIMENSIONNELLE; LIGAND FLUORESCENCE SPECTROSCOPY; URINARY PROTEINS; NASAL-MUCOSA; AFFINITIES; MECHANISM; LIPOCALIN; MOSQUITOS; RECEPTOR.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0200012319094103&uri=/notices/prodinra1/2010/10/
Registros recuperados: 6
Primeira ... 1 ... Última
 

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