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
2013
Spectral Tuning of Ultraviolet Cone Pigments: An Interhelical Lock Mechanism
Sekharan S, Mooney V, Rivalta I, Kazmi M, Neitz M, Neitz J, Sakmar T, Yan E, Batista V. Spectral Tuning of Ultraviolet Cone Pigments: An Interhelical Lock Mechanism. Journal Of The American Chemical Society 2013, 135: 19064-19067. PMID: 24295328, PMCID: PMC4536979, DOI: 10.1021/ja409896y.Peer-Reviewed Original ResearchConceptsUV pigmentsCone pigmentsSpectral tuningActivation of rhodopsinAncestral pigmentMolecular evolutionVertebrate visionMutagenesis studiesPhotoreceptor rhodopsinMolecular levelStructural rearrangementsUnprotonated Schiff baseTransmembraneTM6PigmentsRhodopsinMutationsEssential componentRetinyl chromophoreHydrogen bonding networkMutantsTM2Structural modelPhysiologicalRearrangement