2022
Rational design of photosynthetic reaction center protein maquettes
Ennist N, Stayrook S, Dutton P, Moser C. Rational design of photosynthetic reaction center protein maquettes. Frontiers In Molecular Biosciences 2022, 9: 997295. PMID: 36213121, PMCID: PMC9532970, DOI: 10.3389/fmolb.2022.997295.Peer-Reviewed Original ResearchNatural photosystemsCrystal structureSolar-to-fuel energy conversionAssemble metal ionsElectron-transfer reactionsPhotosynthetic charge separationPhotosynthetic reaction centersCharge separationElectron tunneling theoryChemical fuelsMetal ionsReaction centerElectron donorHolo-stateStructural transitionEnergy conversionElectron acceptorModular strategySpectroscopic assaysReactionPhoton energyCrystalState of assemblyProtein designProduction of biofuelsDe novo protein design of photochemical reaction centers
Ennist N, Zhao Z, Stayrook S, Discher B, Dutton P, Moser C. De novo protein design of photochemical reaction centers. Nature Communications 2022, 13: 4937. PMID: 35999239, PMCID: PMC9399245, DOI: 10.1038/s41467-022-32710-5.Peer-Reviewed Original ResearchConceptsCharge separationSolar-to-fuel energy conversionReaction centerLight-driven charge separationX-ray crystal structurePhotosynthetic reaction center proteinCharge separation lifetimeSolar fuel productionTransient absorption spectroscopyPhotosynthetic reaction centersPhotochemical charge separationModify natural proteinsPhotochemical reaction centerReaction center proteinCluster oxidationRedox centersCrystal structureAbsorption spectroscopyElectron transfer activityNatural protein structuresDe novo protein designPhotosynthetic protein complexesEnergy conversionX-rayProtein framework
2016
Structural Basis for the Procofactor to Cofactor Transition in Human Factor V
Kumar S, Deng W, Stayrook S, Li R, Camire R, Krishnaswamy S. Structural Basis for the Procofactor to Cofactor Transition in Human Factor V. Blood 2016, 128: 253. DOI: 10.1182/blood.v128.22.253.253.Peer-Reviewed Original ResearchBasic regionB domainC-terminusLong standing puzzleBR bindingCrystal structureDocking studiesBr fragmentsHuman factor VCentral B domainA2 domainAmide proton exchange ratesPhosphatidylserine-containing membranesAr2Hydrogen-deuterium exchangeA1-A2-B-A3-C1-C2Adjacent regionsAmide proton exchangeComputational docking studiesProton exchange ratesDomain organizationAcid sequenceProteolytic excisionCofactor formationPrimary structure
2008
Crystal structure of the λ repressor and a model for pairwise cooperative operator binding
Stayrook S, Jaru-Ampornpan P, Ni J, Hochschild A, Lewis M. Crystal structure of the λ repressor and a model for pairwise cooperative operator binding. Nature 2008, 452: 1022-1025. PMID: 18432246, DOI: 10.1038/nature06831.Peer-Reviewed Original ResearchStructural basis for the function and inhibition of an influenza virus proton channel
Stouffer A, Acharya R, Salom D, Levine A, Di Costanzo L, Soto C, Tereshko V, Nanda V, Stayrook S, DeGrado W. Structural basis for the function and inhibition of an influenza virus proton channel. Nature 2008, 451: 596-599. PMID: 18235504, PMCID: PMC3889492, DOI: 10.1038/nature06528.Peer-Reviewed Original Research
2007
Structural Analysis of Lac Repressor Bound to Allosteric Effectors
Daber R, Stayrook S, Rosenberg A, Lewis M. Structural Analysis of Lac Repressor Bound to Allosteric Effectors. Journal Of Molecular Biology 2007, 370: 609-619. PMID: 17543986, PMCID: PMC2715899, DOI: 10.1016/j.jmb.2007.04.028.Peer-Reviewed Original ResearchConceptsHydrogen bond networkHydrogen bondsExtensive hydrogen-bonding networkWater-mediated hydrogen bond networkSugar ringBond networkCrystal structureHydroxyl groupsAllosteric transitionEffector moleculesAnti-inducerSmall moleculesAtomic detailMoleculesStructural conformationC-terminal sub-domainBondsApo-repressorHydrogenHydroxylRepressor functionLac operonLac repressorN-terminalRepressor
2006
The Structure of a Designed Diiron(III) Protein: Implications for Cofactor Stabilization and Catalysis
Wade H, Stayrook S, DeGrado W. The Structure of a Designed Diiron(III) Protein: Implications for Cofactor Stabilization and Catalysis. Angewandte Chemie International Edition 2006, 45: 4951-4954. PMID: 16819737, DOI: 10.1002/anie.200600042.Peer-Reviewed Original Research
2005
X-ray Structure of a Water-soluble Analog of the Membrane Protein Phospholamban: Sequence Determinants Defining the Topology of Tetrameric and Pentameric Coiled Coils
Slovic A, Stayrook S, North B, DeGrado W. X-ray Structure of a Water-soluble Analog of the Membrane Protein Phospholamban: Sequence Determinants Defining the Topology of Tetrameric and Pentameric Coiled Coils. Journal Of Molecular Biology 2005, 348: 777-787. PMID: 15826670, DOI: 10.1016/j.jmb.2005.02.040.Peer-Reviewed Original ResearchConceptsHeptad sequence repeatSequence repeatWater-soluble variantCoiled-coilSequence determinationTransmembrane proteinsTruncated constructsPentameric transmembrane proteinsReticulum membraneStable tetramersTetrameric structureLeu residuesCrystal structurePentameric formX-ray structureInterfacial hydrogen bondsProteinHydrogen bondsResiduesRepeatsMembrane protein phospholambanGCN4Water-soluble analogX-rayHeptad
2001
Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate † , ‡
Jin Y, Stayrook S, Albert R, Palackal N, Penning T, Lewis M. Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate † , ‡. Biochemistry 2001, 40: 10161-10168. PMID: 11513593, DOI: 10.1021/bi010919a.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAllosteric SiteAmino Acid SequenceBinding SitesCloning, MolecularComputer SimulationCrystallography, X-RayEscherichia coliFluoxetineHumansHydroxysteroid DehydrogenasesModels, MolecularMolecular ConformationMolecular Sequence DataNADPProtein BindingProtein Structure, SecondaryRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidUrsodeoxycholic AcidConceptsRat 3alpha-HSDAldo-keto reductase superfamilyBinding protein complexSteroid binding pocketAlpha/beta barrelBound NADP(+Human typeProtein complexesThree-dimensional structureOxyanion holeAndrogen 5alpha-dihydrotestosteroneBinding proteinStructural basisTransport of bile acidsAKR1C2Ternary complexRat isoformsNADP(+SuperfamilyExtended conformationProstatic productionActive siteIsoformsCrystal structureBile acids