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showing 10 items of 184 documents

Crystal Structure of Perakine Reductase, Founding Member of a Novel Aldo-Keto Reductase (AKR) Subfamily That Undergoes Unique Conformational Changes …

2012

Perakine reductase (PR) catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. Sequence alignment shows that PR is the founder of the new AKR13D subfamily and is designated AKR13D1. The x-ray structure of methylated His(6)-PR was solved to 2.31 Å. However, the active site of PR was blocked by the connected parts of the neighbor symmetric molecule in the crystal. To break the interactions and obtain the enzyme-ligand complexes, the A213W mutant was generated. The atomic structure of His(6)-PR-A213W complex with NADPH was determined at 1.77 Å. Overal…

Models Molecularendocrine systemConformational changeProtein ConformationStereochemistryReductaseCrystallography X-Raycomplex mixturesMethylationBiochemistryProtein Structure SecondaryRauwolfiaEvolution MolecularProtein structurehemic and lymphatic diseasesheterocyclic compoundsMolecular BiologyAldo-keto reductaseCofactor bindingbiologyChemistryorganic chemicalsActive siteCell BiologyEnzyme structureAlcohol OxidoreductasesCrystallographyProtein Structure and Foldingbiology.proteinNADPH bindingSequence AlignmentNADPProtein BindingJournal of Biological Chemistry
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Conformational dynamics of active site loops 5, 6 and 7 of enzyme Triosephosphate Isomerase: A molecular dynamics study

2018

AbstractTriosephosphate Isomerase is a glycolytic enzyme catalyzing the interconversion of Dihydroxyacetone phosphate to Glyceraldehyde-3-phosphate. The active site is comprised of three distinct loops loop-6, loop-7 and loop-8. Based on loop-6 and loop-7 conformation we describe the enzyme as Open TIM and Closed TIM. Various NMR, X-ray crystallography and QM/MM simulation techniques have provided glimpses of individual events of what is essentially a dynamic process. We studied the conformational changes of two distinct loops (loop-6 and loop-7) enveloping the active site, in the presence of natural substrate, reaction intermediates and inhibitor molecules, by means of microsecond atomisti…

Molecular dynamicsCrystallographybiologyChemistrybiology.proteinSubstrate (chemistry)Active siteCrystal structureReaction intermediateDihedral angleLigand (biochemistry)Triosephosphate isomerase
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Minireview: Recent progress in hemocyanin research

2011

This review summarizes recent highlights of our joint work on the structure, evolution, and function of a family of highly complex proteins, the hemocyanins. They are blue-pigmented oxygen carriers, occurring freely dissolved in the hemolymph of many arthropods and molluscs. They are copper type-3 proteins and bind one dioxygen molecule between two copper atoms in a side-on coordination. They possess between 6 and 160 oxygen-binding sites, and some of them display the highest molecular cooperativity observed in nature. The functional properties of hemocyanins can be convincingly described by either the Monod-Wyman-Changeux (MWC) model or its hierarchical extension, the Nested MWC model; the…

Molecular modelEcologymedicine.medical_treatmentAllosteric regulationActive siteHemocyaninCooperativityPlant ScienceBiologyAffinitiesHemolymphbiology.proteinmedicineBiophysicsAnimal Science and ZoologyOxygen bindingIntegrative and Comparative Biology
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Calculation of binding energy using BLYP/MM for the HIV-1 integrase complexed with the S-1360 and two analogues.

2007

Abstract Integrase (IN) is one of the three human immunodeficiency virus type 1 (HIV-1) enzymes essential for effective viral replication. S-1360 is a potent and selective inhibitor of HIV-1 IN. In this work, we have carried out molecular dynamics (MD) simulations using a hybrid Quantum Mechanics/Molecular Mechanics (QM/MM) approach, to determine the protein–ligand interaction energy for S-1360 and two analogues. Analysis of the MD trajectories reveals that the strongest protein–inhibitor interactions, observed in the three studied complexes, are established with Lys-159 residue and Mg 2+ cation. Calculations of binding energy using BLYP/MM level of theory reveal that there is a direct rela…

Molecular modelStereochemistryProtein ConformationClinical BiochemistryBinding energyPharmaceutical ScienceHIV IntegraseCrystallography X-RayBiochemistryMolecular mechanicsMolecular dynamicsPropaneStructure-Activity RelationshipDrug DiscoveryHumansMagnesiumPyrrolesAmino Acid SequenceHIV Integrase InhibitorsFuransMolecular Biologychemistry.chemical_classificationbiologyChemistryLysineOrganic ChemistryActive siteInteraction energyTriazolesIntegraseEnzymeAmino Acid SubstitutionModels Chemicalbiology.proteinMolecular MedicineBioorganicmedicinal chemistry
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9 Å cryo-EM structure and molecular model of a gastropod hemocyanin didecamer (KLH1) reveals the architecture of the asymmetric collar

2008

Hemocyanins are blue copper proteins that transport oxygen in the hemolymph of many arthropods and molluscs. Molluscan hemocyanins are decamers, didecamers or multidecamers of a 350–400 kDa polypeptide subunit that is subdivided into seven or eight different functional units (FUs, each with a single copper active site). The quaternary structure is a semi-hollow cylinder consisting of a wall and a collar. Recently, we published a 9 A cryo-EM structure and molecular model of a cephalopod hemocyanin decamer (NpH, from Nautilus pompilius) that answered many hitherto unsolved questions concerning the quaternary structure of molluscan hemocyanin. Notably, it revealed the twisted pathway of the 10…

Molecular modelbiologyChemistryStereochemistryCopper proteinmedicine.medical_treatmentProtein subunitActive siteHemocyaninAnatomybiology.organism_classificationCephalopodHemolymphbiology.proteinmedicineProtein quaternary structure
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Diene-Containing Half-Sandwich MoIII Complexes as Ethylene Polymerization Catalysts: Experimental and Theoretical Studies

2001

International audience; Seventeen-electron compounds of Mo III having the general formula [(h 5-C 5 R 5)Mo(h 4-diene)X 2 ] (R H, Me; diene butadiene, iso-prene, or 2,3-dimethylbutadiene; X Cl, CH 3) are a new class of ethylene polymerization catalysts. The polyethy-lene obtained shows a bimodal distribution , the major weight fraction being characterized by very long (M around 10 6) and highly linear polymer chains. The newly prepared pentamethylcyclo-pentadienyl (Cp*) derivatives are more active than the cyclopentadienyl (Cp) derivatives, but much less active than previously investigated niobium III compounds having the same stoichiometry. On the other hand, the turnover frequency of the a…

MolybdenumAgostic interactionEthylene polymerizationChain propagationbiologyChemistryNiobiumOrganic ChemistryActive site[CHIM.CATA]Chemical Sciences/CatalysisGeneral ChemistryPhotochemistryHeterolysisCatalysisDensity functional calculationsCrystallography[CHIM.POLY]Chemical Sciences/PolymersCyclopentadienyl complexPolymerizationbiology.protein[CHIM.COOR]Chemical Sciences/Coordination chemistryDensity functional theoryMulliken population analysisCyclopentadienyl ligandsChemistry - A European Journal
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The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B

2021

Meprin β (Mβ) is a multidomain type-I membrane metallopeptidase that sheds membrane-anchored substrates, releasing their soluble forms. Fetuin-B (FB) is its only known endogenous protein inhibitor. Herein, we analyzed the interaction between the ectodomain of Mβ (MβΔC) and FB, which stabilizes the enzyme and inhibits it with subnanomolar affinity. The MβΔC:FB crystal structure reveals a ∼250-kDa, ∼160-Å polyglycosylated heterotetrameric particle with a remarkable glycan structure. Two FB moieties insert like wedges through a “CPDCP trunk” and two hairpins into the respective peptidase catalytic domains, blocking the catalytic zinc ions through an “aspartate switch” mechanism. Uniquely, the …

Multiprotein complexMetallopeptidaseCleavage (embryo)Cell LineMiceProtein structureAnimalsHumansEctoprotein sheddingProtease InhibitorsInhibitionBinding SitesMultidisciplinarybiologyChemistryMetallopeptidaseMetalloendopeptidasesActive siteBiological SciencesSheddaseFetuin-BLepidopteraMolecular Docking SimulationTransmembrane domainEctodomainbiology.proteinBiophysicsProtein structureMultiprotein complexAlzheimer’s diseaseProtein Binding
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Different relaxations in myoglobin after photolysis

2004

To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration in myoglobin (Mb), we measured time-resolved absorption spectra in the Soret region after photolysis of carbon monoxide Mb (MbCO) in the temperature interval 120-260 K and in the time window 350 ns to 200 ms. The spectral contributions of both photolyzed (Mb * ) and liganded Mb (MbCO) have been analyzed by taking into account homogeneous bandwidth, coupling to vibrational modes, and static conformational heterogeneity. We succeeded in separating the “time-dependent” spectral changes, and this work provides possibilities to identify the events in the process of ligand rebinding. KHB is domina…

Myoglobin Molecular Dynamics Simulation active siteAbsorption spectroscopyKineticsAnalytical chemistryThermodynamicsIn Vitro TechniquesKinetic energyLigandschemistry.chemical_compoundAnimalsMultidisciplinaryBinding SitesPhotolysisLigandMyoglobinPhotodissociationTemperatureWhalesBiological SciencesKineticsMyoglobinchemistrySpectrophotometryMolecular vibrationThermodynamicsCarbon monoxide
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Spectral broadening of the Soret band in myoglobin: an interpretation by the full spectrum of low-frequency modes from a normal modes analysis.

2005

In this work the temperature dependence of the Soret band line shape in carbon-monoxy myoglobin is re-analyzed by using both the full correlator approach in the time domain and the frequency domain approach. The new analyses exploit the full density of vibrational states of carbon-monoxy myoglobin available from normal modes analysis, and avoid the artificial division of the entire set of vibrational modes coupled to the Soret transition into "high-frequency" and "low-frequency" subsets; the frequency domain analysis, however, makes use of the so-called short-times approximation, while the time domain one avoids it. Time domain and frequency domain analyses give very similar results, thus s…

Myoglobin Molecular Dynamics Simulation active siteChemistryMyoglobinSpectrum AnalysisAnharmonicityBiophysicsAnalytical chemistryTemperatureGeneral MedicineMolecular physicsVibrationSpectral lineModels ChemicalNormal modeMolecular vibrationFrequency domainComputer SimulationTime domainHarmonic oscillatorDoppler broadeningEuropean biophysics journal : EBJ
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A structural insight into the P1 S1 binding mode of diaminoethylphosphonic and phosphinic acids, selective inhibitors of alanine aminopeptidases

2016

Abstract N′-substituted 1,2-diaminoethylphosphonic acids and 1,2-diaminoethylphosphinic dipeptides were explored to unveil the structural context of the unexpected selectivity of these inhibitors of M1 alanine aminopeptidases (APNs) versus M17 leucine aminopeptidase (LAP). The diaminophosphonic acids were obtained via aziridines in an improved synthetic procedure that was further expanded for the phosphinic pseudodipeptide system. The inhibitory activity, measured for three M1 and one M17 metalloaminopeptidases of different sources (bacterial, human and porcine), revealed several potent compounds (e.g., K i  = 65 nM of 1u for Hs APN). Two structures of an M1 representative (APN from Neisser…

Phosphorous AcidsSwineStereochemistryNeisseria meningitidisCD13 AntigensCrystallography X-RayLigands010402 general chemistry01 natural sciencesAminopeptidaseArticleAminopeptidase NPhosphonic and phosphinic acidsLeucyl AminopeptidaseStructure-Activity RelationshipS1 binding modeDrug DiscoveryAnimalsHumansProtease InhibitorsPharmacologyAlanineBinding Sitesbiology010405 organic chemistryChemistryAminopeptidase NOrganic ChemistryActive siteStructural contextAPN-inhibitor complex structuresDipeptidesGeneral MedicinePhosphinic Acids0104 chemical sciencesMetalloaminopeptidasesPhosphinic Acidsbiology.proteinLeucineSelectivityEuropean Journal of Medicinal Chemistry
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