Search results for "DOMAIN"

showing 10 items of 2485 documents

Characterization of the pleiotropic LysR-type transcription regulator LeuO of Escherichia coli

2019

AbstractLeuO is a pleiotropic LysR-type transcriptional regulator (LTTR) and co-regulator of the abundant nucleoid-associated repressor protein H-NS in Gammaproteobacteria. As other LTTRs, LeuO is a tetramer that is formed by dimerization of the N-terminal DNA-binding domain (DBD) and C-terminal effector-binding domain (EBD). To characterize the Escherichia coli LeuO protein, we screened for LeuO mutants that activate the cas (CRISPR-associated/Cascade) promoter more effectively than wild-type LeuO. This yielded nine mutants carrying amino acid substitutions in the dimerization interface of the regulatory EBD, as shown by solving the EBD’s crystal structure. Superimposing of the crystal str…

Models MolecularProtein domainMutantRepressorPlasma protein bindingBiologymedicine.disease_cause03 medical and health sciencesProtein DomainsTranscription (biology)GeneticsConsensus sequencemedicinePromoter Regions GeneticEscherichia coli030304 developmental biologyGenetics0303 health sciences030306 microbiologyEscherichia coli ProteinsGene regulation Chromatin and EpigeneticsGenetic PleiotropyDNAGene Expression Regulation BacterialDNA-Binding ProteinsMutationNucleic Acid ConformationProtein MultimerizationDeoxyribonuclease IProtein BindingTranscription FactorsNucleic Acids Research
researchProduct

Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy

2007

Reducing body myopathy (RBM) is a rare disorder causing progressive muscular weakness characterized by aggresome-like inclusions in the myofibrils. Identification of genes responsible for RBM by traditional genetic approaches has been impossible due to the frequently sporadic occurrence in affected patients and small family sizes. As an alternative approach to gene identification, we used laser microdissection of intracytoplasmic inclusions identified in patient muscle biopsies, followed by nanoflow liquid chromatography-tandem mass spectrometry and proteomic analysis. The most prominent component of the inclusions was the Xq26.3-encoded four and a half LIM domain 1 (FHL1) protein, expresse…

Models MolecularProteomicsMolecular Sequence DataMuscle ProteinsBiologyTransfectionProteomicsInclusion bodiesMuscular DiseasesmedicineAmino Acid SequenceLaser capture microdissectionInclusion BodiesIntracellular Signaling Peptides and ProteinsCardiac muscleSkeletal muscleGenetic Diseases X-LinkedGeneral MedicineLIM Domain Proteinsmedicine.diseaseCongenital myopathyMolecular biologyFHL1medicine.anatomical_structureMutationMyofibrilResearch Article
researchProduct

Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S.

2011

Cysteine cathepsins mediate proteome homeostasis and have pivotal functions in diseases such as cancer. To better understand substrate recognition by cathepsins B, L, and S, we applied proteomic identification of protease cleavage sites (PICS) for simultaneous profiling of prime and non-prime specificity. PICS profiling of cathepsin B endopeptidase specificity highlights strong selectivity for glycine in P3' due to an occluding loop blocking access to the primed subsites. In P1', cathepsin B has a partial preference for phenylalanine, which is not found for cathepsins L and S. Occurrence of P1' phenylalanine often coincides with aromatic residues in P2. For cathepsin L, PICS identifies 845 …

Models MolecularProteomicsTime Factorsmedicine.medical_treatmentProteolysisCathepsin LPhenylalanineGlycineBiologyBiochemistryCathepsin BPichiaCathepsin BSubstrate SpecificityCathepsin LCathepsin OPeptide LibraryCatalytic DomainmedicineHumansCathepsin SEnzyme AssaysCathepsinProteasemedicine.diagnostic_testGeneral ChemistryHydrogen-Ion ConcentrationMolecular biologyCathepsinsHEK293 CellsBiochemistryProteolysisbiology.proteinCysteinePeptide HydrolasesProtein BindingJournal of proteome research
researchProduct

Monolayer curvature stabilizes nanoscale raft domains in mixed lipid bilayers

2013

According to the lipid raft hypothesis, biological lipid membranes are laterally heterogeneous and filled with nanoscale ordered "raft" domains, which are believed to play an important role for the organization of proteins in membranes. However, the mechanisms stabilizing such small rafts are not clear, and even their existence is sometimes questioned. Here we report the observation of raft-like structures in a coarse-grained molecular model for multicomponent lipid bilayers. On small scales, our membranes demix into a liquid ordered (lo) and a liquid disordered (ld) phase. On large scales, phase separation is suppressed and gives way to a microemulsion-type state that contains nanometer si…

Models MolecularQuantitative Biology - Subcellular ProcessesLiquid ordered phaseLipid BilayersFOS: Physical sciencesCondensed Matter - Soft Condensed Matter010402 general chemistry01 natural sciences03 medical and health sciencesMembrane MicrodomainsPhase (matter)MonolayerLipid bilayer phase behaviorPhysics - Biological PhysicsLipid bilayerLipid raftSubcellular Processes (q-bio.SC)030304 developmental biology0303 health sciencesMultidisciplinaryChemistryRaftElasticity0104 chemical sciencesCrystallographyMembraneModels ChemicalBiological Physics (physics.bio-ph)FOS: Biological sciencesPhysical SciencesBiophysicsSoft Condensed Matter (cond-mat.soft)lipids (amino acids peptides and proteins)
researchProduct

Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.

2013

AbstractIn biological membranes the alignment of embedded proteins provides crucial structural information. The transmembrane (TM) parts have well-defined secondary structures, in most cases α-helices and their orientation is given by a tilt angle and an azimuthal rotation angle around the main axis. The tilt angle is readily visualized and has been found to be functionally relevant. However, there exist no general concepts on the corresponding azimuthal rotation. Here, we show that TM helices prefer discrete rotation angles. They arise from a combination of intrinsic properties of the helix geometry plus the influence of the position and type of flanking residues at both ends of the hydrop…

Models MolecularQuantitative Biology::BiomoleculesPotassium ChannelsRotationChemistryCell MembraneMolecular Sequence DataBiophysicsMembraneMembrane ProteinsBiological membraneRotationTransmembrane proteinPeptide FragmentsProtein Structure SecondaryCore (optical fiber)CrystallographyTransmembrane domainChemical physicsOrientation (geometry)HelixPolarAmino Acid SequenceProtein MultimerizationProtein Structure QuaternaryBiophysical journal
researchProduct

Computational Methods in Developing Quantitative Structure-Activity Relationships (QSAR): A Review

2006

Virtual filtering and screening of combinatorial libraries have recently gained attention as methods complementing the high-throughput screening and combinatorial chemistry. These chemoinformatic techniques rely heavily on quantitative structure-activity relationship (QSAR) analysis, a field with established methodology and successful history. In this review, we discuss the computational methods for building QSAR models. We start with outlining their usefulness in high-throughput screening and identifying the general scheme of a QSAR model. Following, we focus on the methodologies in constructing three main components of QSAR model, namely the methods for describing the molecular structure …

Models MolecularQuantitative structure–activity relationshipbusiness.industryComputer scienceOrganic ChemistryQuantitative Structure-Activity RelationshipQuantitative structureFeature selectionGeneral MedicineMachine learningcomputer.software_genreCombinatorial chemistryField (computer science)Computer Science ApplicationsDomain (software engineering)Molecular descriptorDrug DiscoveryArtificial intelligencebusinesscomputerApplicability domainCombinatorial Chemistry & High Throughput Screening
researchProduct

Promiscuity in alkaline phosphatase superfamily. Unraveling evolution through molecular simulations.

2011

We here present a theoretical study of the alkaline hydrolysis of a phosphodiester (methyl p-nitrophenyl phosphate or MpNPP) in the active site of Escherichia coli alkaline phosphatase (AP), a monoesterase that also presents promiscuous activity as a diesterase. The analysis of our simulations, carried out by means of molecular dynamics (MD) simulations with hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, shows that the reaction takes place through a D(N)A(N) or dissociative mechanism, the same mechanism employed by AP in the hydrolysis of monoesters. The promiscuous activity observed in this superfamily can be then explained on the basis of a conserved reaction mechanism. …

Models MolecularReaction mechanismStereochemistrydnaNAlkaline hydrolysis (body disposal)AlkaliesMolecular Dynamics SimulationBiochemistryMolecular mechanicsCatalysisMolecular dynamicsColloid and Surface ChemistryCatalytic DomainphosphodiesterEscherichia colibiologyChemistryHydrolysisActive siteGeneral ChemistryAlkaline PhosphataseEnzymesEnzyme ActivationPhosphodiester bondbiology.proteinAlkaline phosphataseQuantum Theoryalkaline phosphataseJournal of the American Chemical Society
researchProduct

Topology and accessibility of the transmembrane helices and the sensory site in the bifunctional transporter DcuB of Escherichia coli.

2011

C(4)-Dicarboxylate uptake transporter B (DcuB) of Escherichia coli is a bifunctional transporter that catalyzes fumarate/succinate antiport and serves as a cosensor of the sensor kinase DcuS. Sites and domains of DcuB were analyzed for their topology relative to the cytoplasmic or periplasmic side of the membrane and their accessibility to the water space. For the topology studies, DcuB was fused at 33 sites to the reporter enzymes PhoA and LacZ that are only active when located in the periplasm or the cytoplasm, respectively. The ratios of the PhoA and LacZ activities suggested the presence of 10 or 11 hydrophilic loops, and 11 or 12 α-helical transmembrane domains (TMDs). The central part…

Models MolecularRecombinant Fusion ProteinsMolecular Sequence Datalac operonTopologyBiochemistryProtein Structure SecondaryPolyethylene GlycolsProtein structureBacterial ProteinsCatalytic DomainStilbenesAmino Acid SequenceCysteineBinding sitePeptide sequenceDicarboxylic Acid TransportersEscherichia coli K12ChemistryEscherichia coli ProteinsCell MembranePeriplasmic spaceAlkaline PhosphataseTransmembrane domainMembrane proteinBiochemistryLac OperonEthylmaleimideSulfonic AcidsHydrophobic and Hydrophilic InteractionsCysteineBiochemistry
researchProduct

Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks f…

2015

Δ3,Δ2-Enoyl-CoA isomerases (ECIs) catalyze the shift of a double bond from 3Z- or 3E-enoyl-CoA to 2E-enoyl-CoA. ECIs are members of the crotonase superfamily. The crotonase framework is used by many enzymes to catalyze a wide range of reactions on acyl-CoA thioesters. The thioester O atom is bound in a conserved oxyanion hole. Here, the mode of binding of acyl-CoA substrate analogues to peroxisomalSaccharomyces cerevisiaeECI (ScECI2) is described. The best defined part of the bound acyl-CoA molecules is the 3′,5′-diphosphate-adenosine moiety, which interacts with residues of loop 1 and loop 2, whereas the pantetheine part is the least well defined. The catalytic base, Glu158, is hydrogen-bo…

Models MolecularSaccharomyces cerevisiae ProteinsDouble bondStereochemistryProtein ConformationIsomeraseSaccharomyces cerevisiaeEnoyl CoA isomeraseThioesterPhotochemistryDodecenoyl-CoA Isomerasebeta-oxidationSubstrate SpecificityStructural Biologyddc:570Catalytic DomainEnzyme StabilitySide chainMoietyta116chemistry.chemical_classificationHydrogen bondenoyl-CoA isomeraseta1182Hydrogen BondingGeneral Medicinehydrogen-bond networkcrotonaseoxyanion holechemistryAcyl Coenzyme AOxyanion holeOxidation-ReductionProtein BindingActa crystallographica. Section D, Biological crystallography
researchProduct

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
researchProduct