Search results for "homology"

showing 10 items of 770 documents

The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins

2006

Abstract The enzyme strictosidine synthase (STR1) from the Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. Moreover, STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ∼2000 compounds in higher plants. The crystal structures of STR1 in complex with its natural substrates tryptamine and secologanin provide structural understanding of the observed substrate preference and identify residues lining the active site surface that contact the substrates. STR1 catalyzes a Pictet-Spengler–type reaction and represents a novel…

Models MolecularTryptamineProtein FoldingStrictosidine synthaseProtein ConformationMolecular Sequence DataSequence alignmentPlant ScienceCatalysisRauwolfiaSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaCarbon-Nitrogen LyasesAmino Acid SequenceResearch ArticlesConserved SequencePlant ProteinsBinding SitesSequence Homology Amino AcidbiologyIndole alkaloidActive siteCell BiologyLyasebiology.organism_classificationTryptamineschemistryBiochemistrybiology.proteinSecologaninSequence AlignmentThe Plant Cell
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Structure of the human filamin A actin-binding domain.

2009

Filamin A (FLNa) is a large dimeric protein that binds to actin filaments via its actin-binding domain (ABD). The crystal structure of this domain was solved at 3.2 A resolution. The domain adopts a closed conformation typical of other ABDs, but also forms a dimer both in crystallization conditions and in solution. The structure shows the localization of the residues mutated in patients with periventricular nodular heterotopia or otopalatodigital syndrome. Structural analysis predicts that mutations in both types of disorder may affect actin binding.

Models Molecularanimal structuresDimerFilaminsmacromolecular substancesFilaminCalponin homology domainCrystallography X-Raychemistry.chemical_compoundContractile ProteinsStructural BiologyFLNAHumansProtein Interaction Domains and MotifsActin-binding proteinProtein Structure QuaternaryActinbiologyMicrofilament ProteinsGeneral MedicineActinschemistryStructural Homology ProteinDomain (ring theory)Mutationbiology.proteinBiophysicsBinding domainProtein BindingActa crystallographica. Section D, Biological crystallography
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NMR structure of hypothetical protein TA0938 from Thermoplasma acidophilum.

2007

Models MolecularbiologySequence Homology Amino AcidChemistryThermoplasmaArchaeal ProteinsArchaeal ProteinsHypothetical proteinThermoplasmaMolecular Sequence DataThermoplasma acidophilumSequence alignmentComputational biologybiology.organism_classificationBiochemistryStructural genomicsProtein Structure TertiaryStructural BiologyAmino Acid SequenceMolecular BiologyPeptide sequenceNuclear Magnetic Resonance BiomolecularSequence AlignmentProteins
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Subunit organization of the abalone Haliotis tuberculata hemocyanin type 2 (HtH2), and the cDNA sequence encoding its functional units d, e, f, g and…

1999

We have developed a HPLC procedure to isolate the two different hemocyanin types (HtH1 and HtH2) of the European abalone Haliotis tuberculata. On the basis of limited proteolytic cleavage, two-dimensional immunoelectrophoresis, PAGE, N-terminal protein sequencing and cDNA sequencing, we have identified eight different 40-60-kDa functional units (FUs) in HtH2, termed HtH2-a to HtH2-h, and determined their linear arrangement within the elongated 400-kDa subunit. From a Haliotis cDNA library, we have isolated and sequenced a cDNA clone which encodes the five C-terminal FUs d, e, f, g and h of HtH2. As shown by multiple sequence alignments, defg of HtH2 correspond structurally to defg from Octo…

Models Molecularfood.ingredientDNA ComplementarySequence analysismedicine.medical_treatmentMolecular Sequence DataOctopodiformesMegathura crenulataBiochemistryEvolution MolecularfoodSequence Analysis ProteinComplementary DNAmedicineAnimalsHaliotisAmino Acid SequenceCloning MolecularProtein Structure QuaternaryPeptide sequenceImmunoelectrophoresisbiologySequence Homology Amino AcidcDNA libraryHelix SnailsProtein primary structureHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationPeptide FragmentsBiochemistryMolluscaHemocyaninsEuropean journal of biochemistry
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The family of the IL-6-type cytokines: specificity and promiscuity of the receptor complexes.

1997

The cytokines IL-6, LIF, CNTF, OSM, IL-11, and CT-1 have been grouped into the family of IL-6-type cytokines, since they all require gp130 for signal transduction. Interestingly, gp130 binds directly to OSM, whereas complex formation with the other cytokines depends on additional receptor subunits. Only limited structural information on these cytokines and their receptors is available. X-ray structures have been solved for the cytokines LIF and CNTF, whose up-up-down-down four-helix bundle is common to all of these cytokines, and for the receptors of hGH and prolactin, which contain two domains with a fibronectin III-like fold. Since cocrystallization and x-ray analysis of the up to four di…

Models Molecularmedicine.medical_treatmentMolecular Sequence DataBiologyBiochemistryMiceInterleukin 20Structural BiologyAntigens CDmedicineCytokine Receptor gp130AnimalsHumansAmino Acid SequenceReceptorMolecular BiologyCommon gamma chainMembrane GlycoproteinsSequence Homology Amino AcidInterleukin-6Rational designReceptors InterleukinGlycoprotein 130Receptors Interleukin-6Cell biologyFibronectinCytokineImmunologybiology.proteinCytokinesSignal transductionProteins
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The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

1997

The psychrotrophic bacterium Pseudomonas fragi was subjected to cold shocks from 30 or 20 to 5 degrees C. The downshifts were followed by a lag phase before growth resumed at a characteristic 5 degrees C growth rate. The analysis of protein patterns by two-dimentional gel electrophoresis revealed overexpression of 25 or 17 proteins and underexpression of 12 proteins following the 30- or 20-to-5 degrees C shift, respectively. The two downshifts shared similar variations of synthesis of 20 proteins. The kinetic analysis distinguished the induced proteins into cold shock proteins (Csps), which were rapidly but transiently overexpressed, and cold acclimation proteins (Caps), which were more or …

Molecular Sequence DataAdaptation BiologicalBiologyMicrobiologyPolymerase Chain Reaction03 medical and health sciencesHeat acclimationBacterial ProteinsPseudomonas fragiHeat shock proteinNucleic AcidsPseudomonasCold acclimationElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequence[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyHeat-Shock ProteinsComputingMilieux_MISCELLANEOUS030304 developmental biologyGel electrophoresis0303 health sciencesBase SequenceSequence Homology Amino Acid030306 microbiologySequence Analysis DNACold-shock domainbiology.organism_classificationMolecular biologyCold shock responseCold TemperatureDNA-Binding Proteins[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryGenes BacterialCarrier ProteinsSequence AnalysisGenome BacterialResearch ArticleProtein Binding
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Molecular Evolution of Apoptotic Pathways: Cloning of Key Domains from Sponges (Bcl-2 Homology Domains and Death Domains) and Their Phylogenetic Rela…

2000

Cells from metazoan organisms are eliminated in a variety of physiological and pathophysiological processes by apoptosis. In this report, we describe the cloning and characterization of molecules from the marine sponges Geodia cydonium and Suberites domuncula, whose domains show a high similarity to those that are found in molecules of the vertebrate Bcl-2 superfamily and of the death receptors. The Bcl-2 proteins contain up to four Bcl-2 homology regions (BH). Two Bcl-2-related molecules have been identified from sponges that are provided with two of those regions, BH1 and BH2, and are termed Bcl-2 homology proteins (BHP). The G. cydonium molecule, BHP1_GC, has a putative size of 28,164, w…

Molecular Sequence DataApoptosisBiologyHomology (biology)Evolution MolecularMolecular evolutionGeneticsAnimalsHumansAnkyrinAmino Acid SequenceCloning MolecularMolecular BiologyGenePhylogenyEcology Evolution Behavior and SystematicsCaenorhabditis eleganschemistry.chemical_classificationGeneticsBase SequenceSequence Homology Amino AcidPhylogenetic treeIntronbiology.organism_classificationPoriferaSuberites domunculaProto-Oncogene Proteins c-bcl-2chemistryPeptidesJournal of Molecular Evolution
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A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

1999

The gene xynC encoding xylanase C from Bacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 3538 bp DNA fragment containing xynC gene was determined, revealing an open reading frame of 3258 bp that encodes a protein of 120,567 Da. A comparison of the deduced amino acid sequence of xylanase C with known beta-glycanase sequences showed that the encoded enzyme is a modular protein containing three different domains. The central region of the enzyme is the catalytic domain, which shows high homology to family 10 xylanases. A domain homologous to family IX cellulose-binding domains is located in the C-terminal region of xylanase C, whilst the N-terminal r…

Molecular Sequence DataBacillusBiologymedicine.disease_causeMicrobiologyHomology (biology)Substrate Specificitychemistry.chemical_compoundCatalytic DomainEnzyme StabilityEscherichia colimedicineXylobioseAmino Acid SequenceCloning MolecularEscherichia coliPeptide sequencechemistry.chemical_classificationEndo-14-beta XylanasesSequence Homology Amino AcidThermophileTemperatureNucleic acid sequenceSequence Analysis DNAXylosidasesEnzymeBiochemistrychemistryGenes BacterialXylanaseSequence AlignmentMicrobiology
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Vibrio sinaloensis sp. nov., isolated from the spotted rose snapper, Lutjanus guttatus Steindachner, 1869.

2008

Nine bacterial strains were studied by means of rep-PCR, 16S rRNA gene sequence analysis, DNA-DNA hybridization and physiological characterization. Typing analysis by means of rep-PCR showed that all nine strains were highly homogeneous, with similarities above 94 %. The strains were isolated from the same geographical area (Mazatlan, Sinaloa state, Mexico) and the same type of host (cultured rose snapper, Lutjanus guttatus), although from different individuals and organs. Comparison of the almost-complete 16S rRNA gene sequences of five strains showed that they belonged to the genus Vibrio and are closely related to the type strains of Vibrio brasiliensis and Vibrio hepatarius, with simila…

Molecular Sequence DataBiologyMicrobiologyMicrobiologyFish DiseasesSpecies SpecificityVibrionaceaeRNA Ribosomal 16SSequence Homology Nucleic AcidAnimalsTypingMexicoEcology Evolution Behavior and SystematicsVibrioPhylogenetic treeNucleic Acid HybridizationGeneral MedicineRibosomal RNAbiology.organism_classification16S ribosomal RNAVibrioPerciformesPhenotypeVibrio InfectionsTaxonomy (biology)BacteriaInternational journal of systematic and evolutionary microbiology
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Papillote and Piopio:DrosophilaZP-domain proteins required for cell adhesion to the apical extracellular matrix and microtubule organization

2005

Adhesion between epithelial cells and extracellular substrates is normally mediated through basal adhesion complexes. However, some cells also possess comparable junctions on their apical surface. Here, we describe two new Drosophila proteins, Piopio and Papillote, that are required for the link between the apical epithelial surface and the overlying apical extracellular matrix (aECM). The two proteins share a zona pellucida (ZP) domain with mammalian aECM components, including the tectorins found in the vertebrate inner ear. Tagged versions of both proteins localized to the apical epithelial surface. Mutations in piopio, papillote and dumpy (another gene encoding a ZP-domain protein) cause…

Molecular Sequence DataBiologyMicrotubulesEpitheliumExtracellular matrixMicrotubuleCell AdhesionmedicineExtracellularAnimalsDrosophila ProteinsWings AnimalAmino Acid SequenceCell adhesionCytoskeletonZona pellucidaMicrotubule nucleationExtracellular Matrix ProteinsSequence Homology Amino AcidMembrane ProteinsEpithelial CellsCell BiologyExtracellular MatrixCell biologyMicroscopy ElectronDrosophila melanogasterPhenotypemedicine.anatomical_structureMicroscopy FluorescenceMutationCarrier ProteinsDrosophila ProteinJournal of Cell Science
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