2024
A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity
Zavala E, Dansereau S, Burke M, Lipchock J, Maschietto F, Batista V, Loria J. A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity. Protein Science 2024, 33: e5009. PMID: 38747379, PMCID: PMC11094782, DOI: 10.1002/pro.5009.Peer-Reviewed Original ResearchConceptsCatalytic activityPhenylphosphonic acidAnalysis of molecular dynamics trajectoriesNMR chemical shiftsSalt bridgesMolecular dynamics trajectoriesC-terminal carboxyl groupChemical shiftsCombination of solution NMRMolecular dynamicsGuanidinium moietyCarboxyl groupsPara-nitrophenylphosphateSolution NMRActive site inhibitorsHistidine phosphataseActive siteElectrostatic interactionsDynamics trajectoriesEnzymatic functionC-terminusGlycine residuesSubstrate affinityBiochemical experimentsBinding affinity
2022
How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM
Wang J, Liu J, Gisriel CJ, Wu S, Maschietto F, Flesher DA, Lolis E, Lisi GP, Brudvig GW, Xiong Y, Batista VS. How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM. Journal Of Structural Biology 2022, 214: 107902. PMID: 36202310, PMCID: PMC10226527, DOI: 10.1016/j.jsb.2022.107902.Peer-Reviewed Original ResearchConceptsCryo-EM mapsAmino acid residuesAcid residuesCryo-electron microscopy mapIndividual amino acid residuesCyanobacteria Synechocystis spPCC 6803Synechocystis spMicroscopy mapsThermosynechococcus elongatusSARS-CoV-2 spike proteinLocal structural changesResiduesSpike proteinAtomic coordinatesElongatusSubunitsSpeciesProteinSpSimilar structureStructural changesInsights into Binding of Single-Stranded Viral RNA Template to the Replication–Transcription Complex of SARS-CoV‑2 for the Priming Reaction from Molecular Dynamics Simulations
Wang J, Shi Y, Reiss K, Allen B, Maschietto F, Lolis E, Konigsberg WH, Lisi GP, Batista VS. Insights into Binding of Single-Stranded Viral RNA Template to the Replication–Transcription Complex of SARS-CoV‑2 for the Priming Reaction from Molecular Dynamics Simulations. Biochemistry 2022, 61: 424-432. PMID: 35199520, PMCID: PMC8887646, DOI: 10.1021/acs.biochem.1c00755.Peer-Reviewed Original ResearchConceptsReplication-transcription complexPriming reactionRNA duplexesTemplate strandRNA templateHigher-order oligomerizationRNA-dependent RNA polymeraseCryo-EM structureRNA primaseViral RNA templateRNA polymerasePrimer synthesisViral transcriptionSecondary structureViral genomeSubunitsMolecular dynamics simulations
2021
A structurally preserved allosteric site in the MIF superfamily affects enzymatic activity and CD74 activation in D-dopachrome tautomerase
Chen E, Reiss K, Shah D, Manjula R, Allen B, Murphy EL, Murphy JW, Batista VS, Bhandari V, Lolis EJ, Lisi GP. A structurally preserved allosteric site in the MIF superfamily affects enzymatic activity and CD74 activation in D-dopachrome tautomerase. Journal Of Biological Chemistry 2021, 297: 101061. PMID: 34384784, PMCID: PMC8405996, DOI: 10.1016/j.jbc.2021.101061.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric SiteAmino Acid SequenceAntigens, Differentiation, B-LymphocyteBinding SitesCatalytic DomainCrystallography, X-RayCytokinesHistocompatibility Antigens Class IIHumansIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsProtein BindingStructure-Activity RelationshipConceptsAllosteric siteDopachrome tautomeraseDynamic regulatory networksEnzymatic activityLow sequence identityLigand-binding siteMultiple ligand-binding sitesNonoverlapping functionsRegulatory networksAllosteric couplingMacrophage migration inhibitory factor (MIF) familyFactor familySequence identityHomolog DStructural basisPrimary sequenceCD74 activationFunctional similarityConformational changesSolution NMRMIF-2X-ray crystallographyCatalytic siteStructural consequencesSolvent channels
2020
Allosteric Impact of the Variable Insert Loop in Vaccinia H1-Related (VHR) Phosphatase
Beaumont VA, Reiss K, Qu Z, Allen B, Batista VS, Loria JP. Allosteric Impact of the Variable Insert Loop in Vaccinia H1-Related (VHR) Phosphatase. Biochemistry 2020, 59: 1896-1908. PMID: 32348128, PMCID: PMC7364816, DOI: 10.1021/acs.biochem.0c00245.Peer-Reviewed Original ResearchConceptsAcid loopVariable insertActive siteActive-site hydrogen bondsInsert regionSolution nuclear magnetic resonanceNuclear magnetic resonanceMillisecond motionsActive site environmentNormal catalytic functionActive site altersMolecular dynamics simulationsActive site loopHydrogen bondsVaccinia H1Asparagine 74Protein tyrosineTyrosine phosphataseRapid kinetic measurementsAllosteric regionActivity of enzymesKinetic measurementsDynamics simulationsConformational motionsInsert loop
2018
Nanosecond Dynamics Regulate the MIF‐Induced Activity of CD74
Pantouris G, Ho J, Shah D, Syed MA, Leng L, Bhandari V, Bucala R, Batista VS, Loria JP, Lolis E. Nanosecond Dynamics Regulate the MIF‐Induced Activity of CD74. Angewandte Chemie International Edition 2018, 57: 7116-7119. PMID: 29669180, PMCID: PMC6282165, DOI: 10.1002/anie.201803191.Peer-Reviewed Original Research
2014
Kinetics of Thermal Activation of an Ultraviolet Cone Pigment
Mooney V, Sekharan S, Liu J, Guo Y, Batista V, Yan E. Kinetics of Thermal Activation of an Ultraviolet Cone Pigment. Journal Of The American Chemical Society 2014, 137: 307-313. PMID: 25514632, DOI: 10.1021/ja510553f.Peer-Reviewed Original ResearchConceptsTransmembrane helix 6UV pigmentsUnprotonated Schiff baseVisual pigmentsCone pigmentsDim-light visionExtracellular loop 2Vertebrate visual pigmentsMolecular evolutionUltraviolet pigmentsOpsin proteinHelix 6Retinyl chromophoreLoop 2UV cone pigmentBovine rhodopsinRod pigmentRhodopsinHydrogen bonding networkSalt bridgeIonone ringPigmentsSchiff base chromophoreSteric restraintsActivation
2013
Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides
Poojari C, Xiao D, Batista V, Strodel B. Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides. Biophysical Journal 2013, 105: 2323-2332. PMID: 24268144, PMCID: PMC3838749, DOI: 10.1016/j.bpj.2013.09.045.Peer-Reviewed Original ResearchConceptsChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyMembrane/water interfaceFrequency generation spectroscopyΒ-sheet secondary structureChannel-forming proteinMolecular dynamics simulationsSimulated SFG spectraAmphiphilic propertiesHuman islet amyloidGeneration spectroscopySFG spectraWater interfaceΒ-sandwichHuman islet amyloid polypeptideIslet β-cellsAmyloid polypeptideWater permeationDynamics simulationsHIAPP aggregatesSecondary structureMembrane permeationIslet amyloid polypeptideΒ-cellsFibrillar structures
2011
Amphiphilic Adsorption of Human Islet Amyloid Polypeptide Aggregates to Lipid/Aqueous Interfaces
Xiao D, Fu L, Liu J, Batista V, Yan E. Amphiphilic Adsorption of Human Islet Amyloid Polypeptide Aggregates to Lipid/Aqueous Interfaces. Journal Of Molecular Biology 2011, 421: 537-547. PMID: 22210153, PMCID: PMC3350761, DOI: 10.1016/j.jmb.2011.12.035.Peer-Reviewed Original ResearchConceptsLipid/aqueous interfaceAqueous interfaceΒ-sheet aggregatesAb initio quantum chemistry calculationsChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyQuantum chemistry calculationsFrequency generation spectroscopyHuman islet amyloid polypeptideHuman islet amyloid polypeptide aggregatesChemistry calculationsAmphiphilic propertiesGeneration spectroscopyΒ-sheetPolypeptide aggregatesIslet amyloid polypeptideΒ-strandsAggregatesAmyloid polypeptideAdsorbAdsorptionSpectroscopyAmyloid proteinInterfacePotential disruptive effectsPharmaceutical formulation affects titanocene transferrin interactions
Buettner K, Snoeberger R, Batista V, Valentine A. Pharmaceutical formulation affects titanocene transferrin interactions. Dalton Transactions 2011, 40: 9580-9588. PMID: 21847473, DOI: 10.1039/c1dt10805k.Peer-Reviewed Original ResearchConceptsTitanocene dichlorideHuman serum transferrinUV/FT-ICR mass spectrometryMolar absorptivityPH-dependent speciationDifferent molar absorptivitiesDFT calculationsSynergistic anionFluorescence quenchingPharmaceutical formulationsMass spectrometryTransfer energyAnticancer activitySerum transferrinAnticancer drugsPhase II human clinical trialsAbsorptivityNMRAnionsHuman clinical trialsDichloridePotential vehicleSpectrometryTi
2004
QM/MM Study of Energy Storage and Molecular Rearrangements Due to the Primary Event in Vision
Gascon J, Batista V. QM/MM Study of Energy Storage and Molecular Rearrangements Due to the Primary Event in Vision. Biophysical Journal 2004, 87: 2931-2941. PMID: 15339806, PMCID: PMC1304767, DOI: 10.1529/biophysj.104.048264.Peer-Reviewed Original ResearchConceptsMolecular rearrangementQuantum mechanics/molecular mechanics (QM/MM) hybrid methodsEnergy storageQM/MM studyPolyene chainEnergy storage mechanismElectronic excitation energiesHigh-resolution structural dataBovine visual rhodopsinMolecular structureMM studyNet positive chargePrimary photochemical eventSchiff baseC13 positionSchiff base linkageStorage mechanismSteric interactionsTrans productsSteric constraintsPreferential senseFirst-principles understandingPositive chargePhotochemical eventsStructural data