2022
Structural Basis for Reduced Dynamics of Three Engineered HNH Endonuclease Lys-to-Ala Mutants for the Clustered Regularly Interspaced Short Palindromic Repeat (CRISPR)-Associated 9 (CRISPR/Cas9) Enzyme
Wang J, Skeens E, Arantes PR, Maschietto F, Allen B, Kyro GW, Lisi GP, Palermo G, Batista VS. Structural Basis for Reduced Dynamics of Three Engineered HNH Endonuclease Lys-to-Ala Mutants for the Clustered Regularly Interspaced Short Palindromic Repeat (CRISPR)-Associated 9 (CRISPR/Cas9) Enzyme. Biochemistry 2022, 61: 785-794. PMID: 35420793, PMCID: PMC9069930, DOI: 10.1021/acs.biochem.2c00127.Peer-Reviewed Original ResearchConceptsShort palindromic repeatsSubstrate specificityPalindromic repeatsAla mutantWT enzymeRNA-binding domainAssociated 9 (Cas9) systemForeign DNA sequencesDNA strandsWild-type enzymeDouble-strand breaksEnhanced substrate specificityHNH active siteDynamics of proteinsType II immunityCas9 proteinDNA substratesDNA sequencesStructural basisMutantsAla substitutionDistinct conformationsSingle LysCatalytic siteEnzyme
2003
Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide Complexes
Xiong Y, Li F, Wang J, Weiner AM, Steitz TA. Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide Complexes. Molecular Cell 2003, 12: 1165-1172. PMID: 14636575, DOI: 10.1016/s1097-2765(03)00440-4.Peer-Reviewed Original ResearchConceptsCCA-adding enzymeClass I CCA-adding enzymeCrystal structureClose evolutionary relationshipAddition of CCAChemical modificationAmino acid sequenceElectrostatic charge distributionNucleic acid templateEvolutionary relationshipsImmature tRNAsCharge distributionDomain architectureNucleotide complexesArcheoglobus fulgidusEnzyme classesTail domainAcid sequenceEnzyme bindsPolymerase domainTRNARelative orientationComplexesEnzymeTerminus
2002
Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP
Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA. Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP. Cell 2002, 111: 815-824. PMID: 12526808, DOI: 10.1016/s0092-8674(02)01115-7.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCrystallography, X-RayCytidine TriphosphateDimerizationDNA Polymerase betaGeobacillus stearothermophilusModels, MolecularMolecular Sequence DataProtein FoldingProtein Structure, TertiaryRNA NucleotidyltransferasesSequence Homology, Amino AcidConceptsCCA-adding enzymeResolution crystal structureDNA polymerase betaImmature tRNAsNew proteinsBase specificityNucleic acid templateBacillus stearothermophilusPalm domainPolymerase betaIncoming ATPTRNAATPTerminusSubunitsCrystal structureActive siteAdditional structural featuresEnzymeCTPStructural featuresComplexesImportant componentTailDomainCrystal Structure of d-Hydantoinase from Bacillus stearothermophilus: Insight into the Stereochemistry of Enantioselectivity † , ‡
Cheon YH, Kim HS, Han KH, Abendroth J, Niefind K, Schomburg D, Wang J, Kim Y. Crystal Structure of d-Hydantoinase from Bacillus stearothermophilus: Insight into the Stereochemistry of Enantioselectivity † , ‡. Biochemistry 2002, 41: 9410-9417. PMID: 12135362, DOI: 10.1021/bi0201567.Peer-Reviewed Original ResearchConceptsD-hydantoinaseExocyclic substituentsTIM-barrel foldStriking structural similarityApo crystal structureSubstrate recognitionBarrel foldCatalytic chemistryStructural comparisonSide-chain precursorBacillus stearothermophilusCrystal structureAmino acidsStructural similarityDihydroorotaseHydantoinsStereochemistrySubstituentsEnantioselectivityEnzymeStereospecific hydrolysisHydrolysisStructureChemistryHydantoinase
2000
Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond
Li F, Wang J, Steitz T. Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond. Journal Of Molecular Biology 2000, 304: 483-492. PMID: 11090289, DOI: 10.1006/jmbi.2000.4189.Peer-Reviewed Original ResearchConceptsActive siteMulti-angle laser lightSmall-angle X-ray scatteringSize exclusion chromatographyX-ray scatteringFurther dimerizationExclusion chromatographyMoleculesDimeric enzymeC basesOligomerization stateTetramerTransfer RNA moleculesLaser lightTRNA moleculesRNA moleculesMonomersPrimer strandChromatographyEnzymeDimersHigh specificityBindingCCA-adding enzymeDimerization