2017
The role of interfacial lipids in stabilizing membrane protein oligomers
Gupta K, Donlan JAC, Hopper JTS, Uzdavinys P, Landreh M, Struwe WB, Drew D, Baldwin AJ, Stansfeld PJ, Robinson CV. The role of interfacial lipids in stabilizing membrane protein oligomers. Nature 2017, 541: 421-424. PMID: 28077870, PMCID: PMC5501331, DOI: 10.1038/nature20820.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBinding SitesCardiolipinsCell MembraneEscherichia coliEscherichia coli ProteinsLigandsLipidsMass SpectrometryMembrane ProteinsModels, MolecularMolecular Dynamics SimulationMoritellaProtein MultimerizationProtein StabilityReceptors, G-Protein-CoupledSodium-Hydrogen ExchangersThermodynamicsThermus thermophilusIntegrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
Landreh M, Marklund EG, Uzdavinys P, Degiacomi MT, Coincon M, Gault J, Gupta K, Liko I, Benesch JL, Drew D, Robinson CV. Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters. Nature Communications 2017, 8: 13993. PMID: 28071645, PMCID: PMC5234078, DOI: 10.1038/ncomms13993.Peer-Reviewed Original ResearchConceptsIon mobility mass spectrometryGas phaseMass spectrometryMobility mass spectrometryMolecular dynamics simulationsCatalysis rateMD simulationsLipid-binding propertiesDynamics simulationsConformational stabilityStable dimerLarge-scale conformational changesSecondary active transportersConformational changesSpectrometryAntiporter NhaAKingdoms of lifeAnnular lipidsNative foldProtein segmentsInter-domain contactsRole of lipidsThermus thermophilusMembrane lipidsNHA2
2013
Cyclic AMP-dependent Protein Lysine Acylation in Mycobacteria Regulates Fatty Acid and Propionate Metabolism*
Nambi S, Gupta K, Bhattacharyya M, Ramakrishnan P, Ravikumar V, Siddiqui N, Thomas AT, Visweswariah SS. Cyclic AMP-dependent Protein Lysine Acylation in Mycobacteria Regulates Fatty Acid and Propionate Metabolism*. Journal Of Biological Chemistry 2013, 288: 14114-14124. PMID: 23553634, PMCID: PMC3656268, DOI: 10.1074/jbc.m113.463992.Peer-Reviewed Original ResearchMeSH KeywordsAcetylesteraseAmino Acid SequenceBacterial ProteinsCoenzyme A LigasesCyclic AMPFatty AcidsGene DeletionGene Expression Regulation, BacterialLysineMass SpectrometryMolecular Sequence DataMutagenesisMycobacterium bovisMycobacterium tuberculosisPropionatesSequence Homology, Amino AcidSignal TransductionConceptsCAMP-dependent mannerAcyl-CoA synthetaseLysine residuesProtein Lysine AcylationLysine acetyltransferaseLysine acylationPosttranslational modificationsImportant lysine residuesFatty acidsBiological processesIntracellular cAMP levelsFADDMultiple substratesCoA synthetasePropionyl-CoAAcetylationBiological organismsRegulatory cycleCritical roleCAMP levelsResiduesBovis bacillus Calmette-GuérinPropionate metabolismMetabolismEukaryotes
2012
A Bioorthogonal Chemoenzymatic Strategy for Defined Protein Dendrimer Assembly
Gupta K, Singh S, Gupta K, Khan N, Sehgal D, Haridas V, Roy RP. A Bioorthogonal Chemoenzymatic Strategy for Defined Protein Dendrimer Assembly. ChemBioChem 2012, 13: 2489-2494. PMID: 23042694, DOI: 10.1002/cbic.201200559.Peer-Reviewed Original ResearchMeSH KeywordsAminoacyltransferasesBacterial ProteinsChemistry Techniques, SyntheticCysteine EndopeptidasesDendrimersHistidineStaphylococcus aureusLipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins
Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins. Journal Of The American Society For Mass Spectrometry 2012, 23: 1716-1728. PMID: 22847390, DOI: 10.1007/s13361-012-0437-4.Peer-Reviewed Original ResearchMeSH KeywordsBacillus subtilisBacterial ProteinsChromatography, High Pressure LiquidLipopeptidesMass SpectrometryPeptides, CyclicConceptsHigh-performance liquid chromatographyMass spectrometryIonization mass spectrometric studyHigh-resolution mass spectrometryDiagnostic fragment ionsResolution mass spectrometryMass spectrometric characterizationMass spectrometric studyChain length variationReversed-phase high-performance liquid chromatographyMS/MS analysisLaser desorption ionizationMass spectrometric analysisLinear precursorsFragment ionsMacrocyclic ringFatty acid chainsPerformance liquid chromatographySpectrometric characterizationGlu replacementSpectrometric studyAcid moietyComplex mixturesDesorption ionizationFatty acid moieties
2011
Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii
Banerjee M, Gupta K, Balaram H, Balaram P. Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii. Rapid Communications In Mass Spectrometry 2011, 25: 1915-1923. PMID: 21698673, DOI: 10.1002/rcm.5058.Peer-Reviewed Original ResearchConceptsMethanocaldococcus jannaschiiTriosephosphate isomeraseDisulfide bond formationIntramolecular disulfide bondsCysteine thiol groupsMonomer molecular massThree-dimensional structureThermophilic enzymesMass spectrometric identificationMS/MS analysisTetrameric enzymeTertiary structureMolecular massDisulfide bridgesDisulfide-bonded moleculesDisulfide bondsMonomeric massJannaschiiCircular dichroismComplete lossSpectrometric identificationIsomeraseEnzymeTryptic digestDa difference