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
2009
Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding
Sharma H, Yu S, Kong J, Wang J, Steitz TA. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 16604-16609. PMID: 19805344, PMCID: PMC2745332, DOI: 10.1073/pnas.0908380106.Peer-Reviewed Original ResearchConceptsColi catabolite gene activator proteinEscherichia coli catabolite gene activator proteinCatabolite gene activator proteinC-helixConformational changesGene activator proteinDNA binding domainsDNA recognition helixEarlier biochemical dataLarge conformational changesSpecific DNA sequencesBinding of cAMPRecognition helixActivator proteinDNA sequencesDNA bindingBinding domainsActive DNAWT structureInactive formInactive structureBiochemical dataDifferent conformationsBindingConformation