Search results for "bacteri"

showing 10 items of 5466 documents

Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane.

2000

We have studied the membrane insertion of ProW, an Escherichia coli inner membrane protein with seven transmembrane segments and a large periplasmic N-terminal tail, into endoplasmic reticulum (ER)-derived dog pancreas microsomes. Strikingly, significant levels of N-tail translocation is seen only when a minimum of four of the transmembrane segments are present; for constructs with fewer transmembrane segments, the N-tail remains mostly nontranslocated and the majority of the molecules adopt an 'inverted' topology where normally nontranslocated parts are translocated and vice versa. N-tail translocation can also be promoted by shortening of the N-tail and by the addition of positively charg…

Models MolecularBioquímicaGlycosylationChromosomal translocationBiologyEndoplasmic ReticulumBiochemistryBacterial ProteinsMembranes (Biologia)MicrosomesEscherichia coliAnimalsInner membranePancreasMolecular BiologyEscherichia coli ProteinsEndoplasmic reticulumMembrane ProteinsSTIM1Periplasmic spaceCell BiologyMolecular biologyTransmembrane proteinCell biologyMembrane proteinMutationCatsMicrosomeATP-Binding Cassette TransportersProteïnesJournal of Biological Chemistry
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The Escherichia coli Envelope Stress Sensor CpxA Responds to Changes in Lipid Bilayer Properties

2015

The Cpx stress response system is induced by various environmental and cellular stimuli. It is also activated in Escherichia coli strains lacking the major phospholipid, phosphatidylethanolamine (PE). However, it is not known whether CpxA directly senses changes in the lipid bilayer or the presence of misfolded proteins due to the lack of PE in their membranes. To address this question, we used an in vitro reconstitution system and vesicles with different lipid compositions to track modulations in the activity of CpxA in different lipid bilayers. Moreover, the Cpx response was validated in vivo by monitoring expression of a PcpxP-gfp reporter in lipid-engineered strains of E. coli. Our comb…

Models MolecularCardiolipinsSurface PropertiesRecombinant Fusion ProteinsGreen Fluorescent ProteinsLipid BilayersArabidopsisPhospholipidBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundBacterial ProteinsGenes ReportermedicineAcholeplasma laidlawiiPhosphorylationLipid bilayerEscherichia coliPlant ProteinsPhosphatidylethanolamineEscherichia coli ProteinsPhosphatidylethanolaminesVesicleGlycosyltransferasesMembrane ProteinsPhosphatidylglycerolsCell biologychemistryMembrane proteinlipids (amino acids peptides and proteins)Protein foldingSignal transductionProtein KinasesProtein Processing Post-TranslationalSignal TransductionBiochemistry
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Copper(II)-Induced Restructuring of ZnuD, a Zinc(II) Transporter from Neisseria meningitidis.

2019

Cluster 2 (288HDDDNAHAHTH298) from Neisseria meningitidis ZnuD is a flexible loop that captures zinc(II) ions, acting as a "fishing net". We describe its Zn(II) and Cu(II) binding capabilities, focusing on the thermodynamics of such interactions and comparing them with the complexes of the 1MAHHHHHHL9-NH2 region. Copper(II) complexes with the studied ZnuD regions are thermodynamically more stable than the zinc(II) ones-Cu(II) complexes dominate in solution even in close to physiological ratios of the studied metal ions (a 10-fold excess of Zn(II) over Cu(II)). While the binding of native Zn(II) has no significant impact on the structure of its transporter, Cu(II) binding induces a conformat…

Models MolecularConformational changeMetal ions in aqueous solutionchemistry.chemical_elementZincNeisseria meningitidis010402 general chemistry01 natural sciencesInorganic ChemistryBacterial ProteinsHumansProlineAmino Acid SequencePhysical and Theoretical ChemistryCation Transport ProteinsPolyproline helix010405 organic chemistryTransporterCopper0104 chemical sciencesMeningococcal InfectionsCrystallographyZincchemistryHelixThermodynamicsCopperProtein BindingInorganic chemistry
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Targeting the Class A Carbapenemase GES-5 via Virtual Screening

2020

The worldwide spread of &beta

Models MolecularDrugantibiotic resistanceGES-5Antibiotic resistancemedia_common.quotation_subjectIn silicoDrug Evaluation Preclinicallcsh:QR1-502Guyana extended-spectrum-β-lactamaseMicrobial Sensitivity TestsComputational biologyBiologyBiochemistrybeta-LactamasesArticlelcsh:Microbiologyguyana extended-spectrum-β-lactamasecarbapenemase03 medical and health sciencesAntibiotic resistanceBacterial ProteinsDrug Resistance BacterialHumansAntibiotic resistance; GES-5; Guyana extended-spectrum-β-lactamase; carbapenemase; virtual screening; docking; noncovalent inhibitionges-5noncovalent inhibitionMolecular Biology030304 developmental biologymedia_common0303 health sciencesVirtual screening030306 microbiologyAntibiotic resistance; Carbapenemase; Docking; GES-5; Guyana extended-spectrum-β-lactamase; Noncovalent inhibition; Virtual screeningHit to leadvirtual screeningAntimicrobialAnti-Bacterial AgentsCarbapenemsdockingBiomolecules
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Solution Structure of the R3H Domain from Human Sμbp-2

2003

The R3H domain is a conserved sequence motif, identified in over 100 proteins, that is thought to be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. In this work the 3D structure of the R3H domain from human Smubp-2 was determined by NMR spectroscopy. It is the first 3D structure determination of an R3H domain. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet and two alpha-helices, which is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. The similarities are non-trivial, as the amino acid identities are below 10%. Three conserved basic residues cluster o…

Models MolecularEGF-like domainMolecular Sequence DataProtein domainProkaryotic Initiation Factor-3Immunoglobulin domainStructure-Activity RelationshipBacterial ProteinsStructural BiologyEVH1 domainHumansAmino Acid SequenceB3 domainNuclear Magnetic Resonance BiomolecularMolecular BiologyChemistryEscherichia coli ProteinsDHR1 domainProtein Structure TertiaryDNA-Binding ProteinsSolutionsCrystallographyCyclic nucleotide-binding domainSequence AlignmentTranscription FactorsBinding domainJournal of Molecular Biology
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A new evolutionary paradigm for the Parkinson disease gene DJ-1.

2006

The DJ-1 gene is extensively studied because of its involvement in familial Parkinson disease. DJ-1 belongs to a complex superfamily of genes that includes both prokaryotic and eukaryotic representatives. We determine that many prokaryotic groups, such as proteobacteria, cyanobacteria, spirochaetes, firmicutes, or fusobacteria, have genes, often incorrectly called "Thij," that are very close relatives of DJ-1, to the point that they cannot be clearly separated from the eukaryotic DJ-1 genes by phylogenetic analyses of their sequences. In addition, and contrary to a previous study that suggested that DJ-1 genes were animal specific, we show that DJ-1 genes are found in at least 5 of the 6 ma…

Models MolecularGenes FungalMolecular Sequence DataProtein Deglycase DJ-1Genes PlantAmoebozoaEvolution MolecularPhylogeneticsGeneticsAmino Acid SequenceMolecular BiologyGeneEcology Evolution Behavior and SystematicsPhylogenyChromalveolataGeneticsComparative genomicsOncogene ProteinsPhylogenetic treebiologyIntracellular Signaling Peptides and ProteinsFusobacteriaParkinson Diseasebiology.organism_classificationEukaryotic CellsProkaryotic CellsGenes BacterialSchizosaccharomyces pombeSequence AlignmentMolecular biology and evolution
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Mitochondrially encoded cysteine predicts animal lifespan

2007

Summary The role of genetic factors in the determination of lifespan is undisputed. However, numerous successful efforts to identify individual genetic modulators of longevity have not yielded yet a quantitative measure to estimate the lifespan of a species from scratch, merely based on its genomic constitution. Here, we report on a meta-examination of genome sequences from 248 animal species with known maximum lifespan, including mammals, birds, fish, insects, and helminths. Our analysis reveals that the frequency with which cysteine is encoded by mitochondrial DNA is a specific and phylogenetically ubiquitous molecular indicator of aerobic longevity: long-lived species synthesize respirat…

Models MolecularGeneticsAgingMitochondrial DNAFree Radicalsmedia_common.quotation_subjectLongevityRespiratory chainLongevityComputational BiologyLocus (genetics)Cell BiologyMitochondrionBiologyProtein oxidationDNA MitochondrialGenomeMitochondriaMitochondrial ProteinsAnimalsHumansCysteineAnaerobic bacteriaPhylogenymedia_commonAging Cell
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Structure and Function of CutC Choline Lyase from Human Microbiota Bacterium Klebsiella pneumoniae.

2015

CutC choline trimethylamine-lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde. In humans, TMA is produced exclusively by the intestinal microbiota, and its metabolite, trimethylamine oxide, has been associated with a higher risk of cardiovascular diseases. Therefore, information about the three-dimensional structures of TMA-producing enzymes is important for microbiota-targeted drug discovery. We have cloned, expressed, and purified the CutC GRE and the activating enzyme CutD from Klebsiella pneumoniae, a representative of the human microbiota. We have determined the first crystal structures of both the choline-…

Models MolecularKlebsiella pneumoniaeMetaboliteTrimethylamineLyasesmacromolecular substancesBiologydigestive systemBiochemistryMicrobiologyCholinechemistry.chemical_compoundBacterial ProteinsCatalytic DomainCholineChymotrypsinHumansMolecular Biologychemistry.chemical_classificationChymotrypsinMicrobiotaCell Biologybiology.organism_classificationLyaseEnzyme structureProtein Structure TertiaryKlebsiella pneumoniaeEnzymechemistryBiochemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProtein Structure and Foldingbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelProtein MultimerizationThe Journal of biological chemistry
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Signal amplification and transduction in phytochrome photosensors

2014

[Introduction] Page 2 of 20 Sensory proteins must relay structural signals from the sensory site over large distances to regulatory output domains. Phytochromes are a major family of red-light sensing kinases that control diverse cell ular functions in plants, bacteria, and fungi. 1-9 Bacterial phytochro mes consist of a photosensory core and a C-te rminal regulatory domain. 10,11 Structures of photosensory cores are reported in the resting state 12-18 and conformational responses to light activat ion have been proposed in the vicinity of the chromophore. 19-23 However, the structure of the signalling state and the mechanism of downstream signal re lay through the photosensory core remain e…

Models MolecularLight Signal TransductionProtein ConformationCrystallography X-RayArticleProtein structureBacterial Proteinsmolecular biophysicsDeinococcusBinding siteCalcium signalingBinding SitesMultidisciplinarybiokemiabiologyPhytochrometa1182Deinococcus radioduransChromophorebiology.organism_classificationBiochemistryBiophysicsDeinococcusPhytochromeTransduction (physiology)röntgenkristallografiaNature
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Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome.

2020

Phytochromes are photosensory proteins in plants, fungi, and bacteria, which detect red- and far-red light. They undergo a transition between the resting (Pr) and photoactivated (Pfr) states. In bacterial phytochromes, the Pr-to-Pfr transition is facilitated by two intermediate states, called Lumi-R and Meta-R. The molecular structures of the protein in these states are not known and the molecular mechanism of photoconversion is not understood. Here, we apply transient infrared absorption spectroscopy to study the photocycle of the wild-type and Y263F mutant of the phytochrome from Deinococcus radiodurans (DrBphP) from nanoto milliseconds. We identify two sequentially forming Lumi-R states …

Models MolecularLight Signal TransductionSpectrophotometry InfraredspektroskopiaMutantGeneral Physics and AstronomyInfrared spectroscopy010402 general chemistry01 natural sciences03 medical and health scienceschemistry.chemical_compoundProtein structureBacterial ProteinsinfrapunasäteilyPhysical and Theoretical ChemistryTyrosineSpectroscopy030304 developmental biology0303 health sciencesBiliverdinPhytochromebiologyChemistryDeinococcus radioduransbiology.organism_classification0104 chemical sciencesProtein Structure TertiaryMutationBiophysicsproteiinitvalokemiaDeinococcusPhytochromePhysical chemistry chemical physics : PCCP
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