Search results for "Protein superfamily"

showing 10 items of 14 documents

Large clostridial cytotoxins — a family of glycosyltransferases modifying small GTP-binding proteins

1996

Some Clostridium species produce AB x -type protein cytotoxins of high molecular weight. These toxins constitute the group of large clostridial cytotoxins (LCTs), which have homologous protein sequences, exert glycosyltransferase activity and modify GTP-binding proteins of the Ras-superfamily. These characteristics render the LCTs valuable tools for developmental and cell biologists.

ClostridiumMicrobiology (medical)Clostridium speciesMicrobial toxinsCytotoxinsBacterial ToxinsCellGlycosyltransferasesProtein superfamilyBiologyGlycosyltransferase activityMicrobiologyInfectious DiseasesGTP-binding protein regulatorsmedicine.anatomical_structureBiochemistryVirologyGlycosyltransferaseras Proteinsbiology.proteinmedicineCytotoxicityTrends in Microbiology
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Identification, molecular cloning, and phylogenetic analysis of a non-respiratory pseudo-hemocyanin of Homarus americanus.

1999

Copper-containing hemocyanins serve to transport oxygen in many arthropod species. Here I describe the identification and cDNA cloning of a structurally closely related non-respiratory pseudo-hemocyanin (PHc) of the American lobster, Homarus americanus. This protein has lost the ability to bind copper and, therefore, oxygen because a histidine residue in copper-binding site A is replaced by tyrosine. Like many arthropod hemocyanins, PHc forms a hexamer. It consists of two different subunit types of 660 and 661 amino acids, respectively, that share a 94.4% sequence identity. Whereas Homarus hemocyanin is produced in the hepatopancreas, PHc is synthesized by the ovaries and the heart tissue. …

DNA ComplementaryProtein subunitmedicine.medical_treatmenteducationMolecular Sequence Datachemical and pharmacologic phenomenaMolecular cloningBiologybehavioral disciplines and activitiesBiochemistryPhylogeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequencePhylogenychemistry.chemical_classificationHomarusBase SequenceSequence Homology Amino AcidEcologyHemocyaninCell BiologyProtein superfamilybiology.organism_classificationAmino acidNephropidaeMicroscopy ElectronBiochemistrychemistryHemocyaninsThe Journal of biological chemistry
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Other astacin homologs

2013

Publisher Summary This chapter describes the activity, specificity and structural chemistry of astacin homologs. The astacins are members of the metzincin superfamily such as the serralysins, the reprolysins/adamalysins, the matrixins, the leishmanolysins, the pregnancy-associated plasma proteins, the snapalysins and the fragilysins. Proteins of the hatching subfamily have been shown to be important for the cleavage of membranes coating developing embryos of invertebrates and vertebrates. Other members of this subfamily have varying or even several functions. UVS.2 from Xenopus, originally shown to play a role in dorso-anterior development, has been identified as the frog hatching enzyme. T…

GeneticsMessenger RNASubfamilyEmbryogenesisXenopusEmbryoProtein superfamilyBiologybiology.organism_classificationMolecular biologyCell biologyembryonic structuresHomologous chromosomeAstacin
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Effects of nucleotide binding to LmrA: A combined MAS-NMR and solution NMR study

2015

ABC transporters are fascinating examples of fine-tuned molecular machines that use the energy from ATP hydrolysis to translocate a multitude of substrates across biological membranes. While structural details have emerged on many members of this large protein superfamily, a number of functional details are still under debate. High resolution structures yield valuable insights into protein function, but it is the combination of structural, functional and dynamic insights that facilitates a complete understanding of the workings of their complex molecular mechanisms. NMR is a technique well-suited to investigate proteins in atomic resolution while taking their dynamic properties into account…

Magnetic Resonance SpectroscopyBiophysicsATP-binding cassette transporterProtein dynamicsCrystallography X-RayBiochemistryLmrABacterial ProteinsNucleotide bindingMagic angle spinningSolution NMRNucleotidesChemistryWalker motifsCell BiologyNuclear magnetic resonance spectroscopyProtein superfamilyBiochemistryCyclic nucleotide-binding domainBiophysicsMAS NMRABC transporterMultidrug Resistance-Associated ProteinsMultidrug Resistance-Associated ProteinsHeteronuclear single quantum coherence spectroscopyProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Simulated annealing with restrained molecular dynamics using CONGEN: Energy refinement of the NMR solution structures of epidermal and type-αtransfor…

1996

The new functionality of the program CONGEN (Bruccoleri RE, Karplus M, 1987, Biopolymers 26:137-168; Bassolino-Klimas D et al., 1996, Protein Sci 5:593-603) has been applied for energy refinement of two previously determined solution NMR structures, murine epidermal growth factor (mEGF) and human type-alpha transforming growth factor (hTGF alpha). A summary of considerations used in converting experimental NMR data into distance constraints for CONGEN is presented. A general protocol for simulated annealing with restrained molecular dynamics is applied to generate NMR solution structures using CONGEN together with real experimental NMR data. A total of 730 NMR-derived constraints for mEGF a…

Maxima and minimaMolecular dynamicsCrystallographyProtein structureChemistrySimulated annealingMoleculeNuclear magnetic resonance spectroscopyProtein superfamilyType (model theory)Molecular BiologyBiochemistryProtein Science
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Crystal structure of the infectious phenotype-associated outer surface protein BBA66 from the Lyme disease agent Borrelia burgdorferi

2014

Borrelia burgdorferi, the causative agent of Lyme disease is transmitted to the mammalian host organisms by infected Ixodes ticks. Transfer of the spirochaetal bacteria from Ixodes ticks to the warm-blooded mammalian organism provides a challenge for the bacteria to adapt and survive in the different environmental conditions. B. burgdorferi has managed to differentially express genes in response to the encountered changes such as temperature and pH variance or metabolic rate to survive in both environments. In recent years, much interest has been turned on genes that are upregulated during the borrelial transfer to mammalian organisms as this could reveal the proteins important in the patho…

Models MolecularMolecular Sequence DataSequence alignmentCrystallography X-RayMicrobiologyMicrobiologyLyme diseasemedicineAnimalsAmino Acid SequenceBorrelia burgdorferiGeneAntigens BacterialLyme DiseaseIxodesbiologyProtein superfamilybiology.organism_classificationmedicine.diseasePhenotypeInfectious DiseasesMembrane proteinBorrelia burgdorferiInsect ScienceParasitologyIxodesSequence AlignmentBacterial Outer Membrane ProteinsTicks and Tick-borne Diseases
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Structural characterization of the Borrelia burgdorferi outer surface protein BBA73 implicates dimerization as a functional mechanism.

2013

Borrelia burgdorferi, which is the causative agent of Lyme disease, is transmitted from infected Ixodes ticks to a mammalian host following a tick bite. Upon changing the host organism from an Ixodes tick to a warm-blooded mammal, the spirochete must adapt to very different conditions, which is achieved by altering the expression of several genes in response to a changing environment. Recently, considerable attention has been devoted to several outer surface proteins, including BBA73, that undergo dramatic upregulation during the transmission of B. burgdorferi from infected Ixodes ticks to mammals and that are thought to be important for the establishment and maintenance of the infection. T…

Models MolecularMolecular Sequence DataStatic ElectricityBiophysicsCrystallography X-RayBiochemistryProtein Structure SecondaryMicrobiologyProtein structureAnimalsAmino Acid SequenceBorrelia burgdorferiCloning MolecularProtein Structure QuaternaryMolecular BiologyPeptide sequenceLyme DiseaseBinding SitesbiologyIxodesSequence Homology Amino AcidCell BiologyProtein superfamilyLigand (biochemistry)biology.organism_classificationSolutionsMembrane proteinBorrelia burgdorferiLyme disease microbiologyIxodesProtein MultimerizationBacterial Outer Membrane ProteinsBiochemical and biophysical research communications
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Assessing model accuracy using the homology modeling automatically software

2007

Homology modeling is a powerful technique that greatly increases the value of experimental structure determination by using the structural information of one protein to predict the structures of homologous proteins. We have previously described a method of homology modeling by satisfaction of spatial restraints (Li et al., Protein Sci 1997;6:956-970). The Homology Modeling Automatically (HOMA) web site,http://www-nmr.cabm.rutgers.edu/HOMA, is a new tool, using this method to predict 3D structure of a target protein based on the sequence alignment of the target protein to a template protein and the structure coordinates of the template. The user is presented with the resulting models, togeth…

Models MolecularProtein Conformationbusiness.industryProteinsSequence alignmentStructure validationComputational biologyProtein superfamilyMachine learningcomputer.software_genreBiochemistryHomology (biology)Structural genomicsProtein structureStructural BiologyArtificial intelligenceTarget proteinHomology modelingbusinessMolecular BiologycomputerSoftwareMathematicsProteins: Structure, Function, and Bioinformatics
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Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: application in predi…

1997

We have developed an automatic approach for homology modeling using restrained molecular dynamics and simulated annealing procedures, together with conformational search algorithms available in the molecular mechanics program CONGEN (Bruccoleri RE, Karplus M, 1987, Biopolymers 26:137-168). The accuracy of the method is validated by "predicting" structures of two homeodomain proteins with known three-dimensional structures, and then applied to predict the three-dimensional structure of the homeodomain of the murine Msx-1 transcription factor. Regions of the unknown protein structure that are highly homologous to the known template structure are constrained by "homology distance constraints,"…

Models MolecularSaccharomyces cerevisiae ProteinsProtein ConformationMSX1 Transcription FactorMolecular Sequence DataSaccharomyces cerevisiaeBiologyProtein EngineeringBiochemistryProtein Structure SecondaryMolecular dynamicsMiceProtein structureAnimalsComputer SimulationHomology modelingAmino Acid SequenceMolecular BiologyHomeodomain ProteinsMSX1 Transcription FactorSequence Homology Amino AcidNuclear ProteinsProtein engineeringProtein superfamilyengrailedRepressor ProteinsCrystallographyAntennapedia Homeodomain ProteinThreading (protein sequence)AlgorithmsInformation SystemsTranscription FactorsResearch ArticleProtein science : a publication of the Protein Society
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2015

Pseudomonas aeruginosa is a Gram-negative bacterium known to cause opportunistic infections in immune-compromised or immunosuppressed individuals that often prove fatal. New drugs to combat this organism are therefore sought after. To this end, we subjected the gene products of predicted perturbative genes to structure-based druggability predictions using DrugPred. Making this approach suitable for large-scale predictions required the introduction of new methods for calculation of descriptors, development of a workflow to identify suitable pockets in homologous proteins and establishment of criteria to obtain valid druggability predictions based on homologs. We were able to identify 29 pert…

MultidisciplinaryPseudomonas aeruginosaDrug discoveryDruggabilityComputational biologyProtein superfamilyBiologymedicine.disease_causechEMBLGenomeMicrobiologymedicineGeneOrganismPLOS ONE
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