Search results for "Protein S"

showing 10 items of 1431 documents

Identification of the membrane penetrating domain of Vibrio cholerae cytolysin as a β-barrel structure

2005

Summary Vibrio cholerae cytolysin (VCC) is an oligomerizing pore-forming toxin that is related to cytolysins of many other Gram-negative organisms. VCC contains six cysteine residues, of which two were found to be present in free sulphydryl form. The positions of two intramolecular disulphide bonds were mapped, and one was shown to be essential for correct folding of protoxin. Mutations were created in which the two free cysteines were deleted, so that single cysteine substitution mutants could be generated for site-specific labelling. Employment of polarity-sensitive fluorophores identified amino acid side-chains that formed part of the pore-forming domain of VCC. The sequence commenced at…

chemistry.chemical_classificationStereochemistryBiologymedicine.disease_causeAntiparallel (biochemistry)MicrobiologyAmino acidBiochemistrychemistryVibrio choleraemedicineCytolysinLipid bilayerMolecular BiologyPeptide sequenceProtein secondary structureCysteineMolecular Microbiology
researchProduct

Predicted secondary structure of hydroperoxide lyase from green bell pepper cloned in the yeast Yarrowia lipolytica

2010

International audience; Fatty acid hydroperoxide lyase (HPL) is a member of the cytochrome P450 family acting on fatty acid hydroperoxides in many organisms. The active green bell pepper HPL, cloned and expressed in the yeast Yarrowia lipolytica, was purified by immobilized metal-ion affinity chromatography (IMAC) in the presence of 2% of Triton X-100R. The secondary structure prediction by bioinformatics servers of HPL was realized by ANTHEPROT software, using the GOR, DPM and Predator methods. The theoretical results which are average values obtained from three different calculation methods showed 33% α-helix, 18% β-sheet, 7% turn and 42% coil. On the other hand, the secondary structure a…

chemistry.chemical_classificationYarrowia lipolyticaCircular dichroismChromatographybiologyProcess Chemistry and Technology[SDV]Life Sciences [q-bio]Circular dichroism spectroscopyBioengineeringYarrowiabiology.organism_classificationBiochemistryCatalysisYeastRandom coilHydroperoxide lyaseEnzymeAffinity chromatographyBiochemistrychemistrySecondary structureSpecific activityPredictionProtein secondary structure
researchProduct

Acetylcholine esterase: the structure.

1991

chemistry.chemical_classificationbiologyMolecular StructureSpatial structureProtein ConformationActive siteBiochemistryAcetylcholinesteraseAcetylcholine esterasechemistry.chemical_compoundEnzymeProtein structurechemistryBiochemistrybiology.proteinAcetylcholinesteraseMolecular BiologyTrends in biochemical sciences
researchProduct

The Formation of The Plant Vacuolar System

1999

The plant vacuole is a multifunctional subcellular compartment. In general, the vacuolar system is constituted of a single or few vacuoles. About 80% of the volume of mature plant cells is occupied by vacuoles. These organelles are limited by a single membrane, the tonoplast. According to the cell type and to particular functions, the vacuolar content can vary from a homogeneous consistency to a heterogeneous matrix containing crystalloid structures (Boiler, Wiemken, 1986; Marty et al., 1980). From the biotechnological point of view, the endomembrane system of plants, particularly the ER and vacuoles, can be envisioned as the ultimate environment for stable protein accumulation. Several rep…

chemistry.chemical_classificationchemistryfungiOrganelleProtein storage vacuolefood and beveragesStorage proteinEndomembrane systemVacuoleCompartment (chemistry)Matrix (biology)Plant cellCell biology
researchProduct

Measurement of Protein Synthesis: In Vitro Comparison of 68Ga-DOTA-Puromycin, [3H]Tyrosine, and 2-Fluoro-[3H]tyrosine

2012

Aim: Puromycin has played an important role in our understanding of the eukaryotic ribosome and protein synthesis. It has been known for more than 40 years that this antibiotic is a universal protein synthesis inhibitor that acts as a structural analog of an aminoacyl-transfer RNA (aa-tRNA) in eukaryotic ribosomes. Due to the role of enzymes and their synthesis in situations of need (DNA damage, e.g., after chemo- or radiation therapy), determination of protein synthesis is important for control of antitumor therapy, to enhance long-term survival of tumor patients, and to minimize side-effects of therapy. Multiple attempts to reach this goal have been made through the last decades, mostly u…

chemistry.chemical_classificationchemistry.chemical_compoundEnzymeProtein synthesis inhibitorchemistryBiochemistryPuromycinProtein biosynthesisTyrosineCycloheximideRibosomeAmino acid
researchProduct

Conformation of dehydropentapeptides containing four achiral amino acid residues - controlling the role of L-valine.

2014

Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.

chemistry.chemical_classificationconformationdehydropeptideChemistryStereochemistryOrganic ChemistryPeptideNuclear magnetic resonance spectroscopydehydroalaninedehydrophenylalanineFull Research PaperNMRlcsh:QD241-441Residue (chemistry)chemistry.chemical_compoundChemistrylcsh:Organic chemistryDehydroalanineValinelcsh:QAmino acid residuelcsh:ScienceProtein secondary structureBeilstein journal of organic chemistry
researchProduct

Identification of Gip as a novel phage-encoded gyrase inhibitor protein featuring a broad activity profile

2021

AbstractBacteriophages represent a powerful source for the identification of novel antimicrobial proteins. In this study, a screening of small cytoplasmic proteins encoded by the CGP3 prophage of Corynebacterium glutamicum, resulted in the identification of the novel gyrase-inhibiting protein Cg1978 (Gip), which shows a direct interaction with the gyrase subunit A (GyrA). In vitro supercoiling assays further suggest a stabilization of the cleavage complex by Gip. Overproduction of Gip in C. glutamicum resulted in a severe growth defect as well as an induction of the SOS response. The cells adapted to gip overexpression by increasing expression levels of gyrAB and by reducing topA expression…

chemistry.chemical_compoundBiochemistrychemistryProtein subunitmedicineDNA supercoilSOS responsemedicine.disease_causeDNA gyraseEscherichia coliProphageDNACorynebacterium glutamicum
researchProduct

ElaC Encodes a Novel Binuclear Zinc Phosphodiesterase

2002

ElaC is a widespread gene found in eubacteria, archaebacteria, and mammals with a highly conserved sequence. Two human ElaC variants were recently associated with cancer (Tavtigian, S. V., Simard, J., Teng, D. H., Abtin, V., Baumgard, M., Beck, A., Camp, N. J., Carillo, A. R., Chen, Y., Dayananth, P., Desrochers, M., Dumont, M., Farnham, J. M., Frank, D., Frye, C., Ghaffari, S., Gupte, J. S., Hu, R., Iliev, D., Janecki, T., Kort, E. N., Laity, K. E., Leavitt, A., Leblanc, G., McArthur-Morrison, J., Pederson, A., Penn, B., Peterson, K. T., Reid, J. E., Richards, S., Schroeder, M., Smith, R., Snyder, S. C., Swedlund, B., Swensen, J., Thomas, A., Tranchant, M., Woodland, A. M., Labrie, F., Sko…

chemistry.chemical_elementZincBiologymedicine.disease_causeBiochemistrybeta-LactamasesHomology (biology)Conserved sequenceGene productEscherichia colimedicineHistidineCloning MolecularBinding siteMolecular BiologyEscherichia coliHistidineCell NucleusIonsBinding SitesModels StatisticalPhosphoric Diester HydrolasesSpectrum AnalysisX-RaysPhosphodiesteraseCell BiologyProtein Structure TertiaryOxygenKineticsZincBiochemistrychemistryChromatography GelProtonsDimerizationProtein BindingJournal of Biological Chemistry
researchProduct

The hedgehog receptor patched is involved in cholesterol transport.

2011

International audience; BACKGROUND: Sonic hedgehog (Shh) signaling plays a crucial role in growth and patterning during embryonic development, and also in stem cell maintenance and tissue regeneration in adults. Aberrant Shh pathway activation is involved in the development of many tumors, and one of the most affected Shh signaling steps found in these tumors is the regulation of the signaling receptor Smoothened by the Shh receptor Patched. In the present work, we investigated Patched activity and the mechanism by which Patched inhibits Smoothened. METHODOLOGY/PRINCIPAL FINDINGS: Using the well-known Shh-responding cell line of mouse fibroblasts NIH 3T3, we first observed that enhancement …

ciliumlcsh:MedicineyeastBiochemistryReceptors G-Protein-CoupledTransmembrane Transport ProteinsMicechemistry.chemical_compound0302 clinical medicineMolecular Cell Biology[SDV.IDA]Life Sciences [q-bio]/Food engineeringMembrane Receptor SignalingBiomacromolecule-Ligand InteractionsSonic hedgehoglcsh:ScienceComputingMilieux_MISCELLANEOUS0303 health sciencesMultidisciplinaryMechanisms of Signal TransductionVeratrum Alkaloids[SDV.IDA] Life Sciences [q-bio]/Food engineeringdrosophilaSmoothened ReceptorLipidsHedgehog signaling pathwayCell biologySterolsSmoothened ReceptorAlimentation et Nutritionembryonic structurescilMembranes and Sorting[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Signal transductionvesicular traffickingSignal TransductionResearch Articleprimary ciliumPatched ReceptorsPatchedsignal-transductionanimal structuresCyclopamine[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringBiophysicsReceptors Cell Surfacepathway activationSaccharomyces cerevisiaetransduction du signalBiology03 medical and health sciencessonic hedgehoglipidAnimalsHumansFood and NutritionHedgehog Proteins[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringBiology030304 developmental biologyPatched Receptorsprotein signalsCell Membranelcsh:RProteinscholesterolBiological TransportTransmembrane Proteinssterol-sensing domainchemistry[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]NIH 3T3 Cellscholesterol;lipid;cell trafficking; yeast;drosophila;cells ; pathway activation; vesicular trafficking; signal-transduction; sonic hedgehog;sterol-sensing domain; primary cilium;protein signalsbiology.proteincellslcsh:Qcell traffickingSmoothened030217 neurology & neurosurgery
researchProduct

Conformational investigation of α,β‐dehydropeptides Part VI. Molecular and crystal structure of benzyloxycarbonylglycyl‐(Z )‐dehydrophenylalanine

1994

The structure of a peptide containing C-terminal dehydrophenylalanine, Z-Gly-(Z)-delta Phe (C19H18N2O5, MW = 354) was determined from single-crystal X-ray diffraction data. Needle-shaped crystals were grown from a 1:1 mixture of methanol-acetone in the monoclinic space group P2(1) with a = 14.717(4), b = 4.941(2), c = 12.073(4) A, beta = 103.72(4) degrees; V = 852.86(8) A3, Z = 2 and Dc = 1.32 g cm-3. The structure was solved by direct methods using SHELXS-86 and refined to a final R-index of 0.032 for 1714 observed reflections. The peptide adopts a conformation folded at the glycine residue, and principal torsion angles are omega 0 = -167.6(2) degrees, phi 1 = -71.8(3) degrees, psi 1 = -31…

conformationdehydropeptidehydrogen bondProtein ConformationChemistryHydrogen bondhelical conformersIntermolecular forceDipeptidesCrystal structuredehydrophenylalanineBiochemistryZ‐Gly‐(Z )‐APheCrystallographyProtein structureX-Ray DiffractionIntramolecular forceSpectroscopy Fourier Transform InfraredX-ray crystallographyMoleculeinfrared spectroscopyX‐ray structure analysisMonoclinic crystal systemInternational Journal of Peptide and Protein Research
researchProduct