2012
Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB
Yu T, Mok K, Kennedy K, Valton J, Anderson K, Walker G, Taga M. Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB. Protein Science 2012, 21: 839-849. PMID: 22528544, PMCID: PMC3403419, DOI: 10.1002/pro.2068.Peer-Reviewed Original ResearchConceptsConserved residuesFlavin mononucleotideReduced catalytic functionPurified mutant proteinsBacterium Sinorhizobium melilotiActive site residuesReduced flavin mononucleotideFlavin isoalloxazine ringCatalytic residuesMutant proteinsFlavin bindingDMB synthesisStructure-function relationshipsActive siteEnzyme familyGenetic screeningSite residuesMutant formsLower axial ligandBound flavinCatalytic functionMutantsEnzyme assaysIsoalloxazine ringBluB
2001
Y265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*
Shah A, Li S, Anderson K, Sweasy J. Y265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*. Journal Of Biological Chemistry 2001, 276: 10824-10831. PMID: 11154692, DOI: 10.1074/jbc.m008680200.Peer-Reviewed Original ResearchConceptsDNA polymerase betaPolymerase betaVivo genetic screenWild-type proteinWild-type enzymeActive site residuesGenetic screenTyr-265Mutant proteinsMutator mutantsPolymerase structureProper geometric alignmentSite residuesProtein conformationNucleotidyl transferForward mutationDNA polymerasePolymerase fidelityDNTP substratesDNA synthesisProteinDeoxynucleoside triphosphatesFirst evidenceTemplate A.Enzyme
1999
Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. Wright
Nagi A, Anderson K, Regan L. Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. Wright. Journal Of Molecular Biology 1999, 286: 257-265. PMID: 9931264, DOI: 10.1006/jmbi.1998.2474.Peer-Reviewed Original ResearchConceptsFour-helix bundle proteinWild-type proteinHelix-connecting loopsProtein folding pathwaysMutant proteinsTwo-residue loopSame general mechanismHelix monomersLength variantsFolding pathwaysE. WrightDimeric intermediateProteinGeneral mechanismFoldingPolyglycine linkerPathwayGlycine linkerLinkerLoop lengthAlterations
1995
Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding
Hoffmann K, Kakalis L, Anderson K, Armitage I, Handschumacher R. Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding. The FEBS Journal 1995, 229: 188-193. PMID: 7744028, DOI: 10.1111/j.1432-1033.1995.0188l.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid IsomerasesBase SequenceBinding SitesCarrier ProteinsCyclophilin DCyclophilinsCyclosporineEnzyme ActivationEscherichia coliHumansMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPeptidylprolyl IsomeraseProtein BindingRecombinant ProteinsConceptsCyP-40Isomerase activityPeptidyl-prolyl cis-trans isomerase activityHuman cyclophilin-40PGEX-3X expression vectorSite-directed mutagenesisMutant proteinsCyclophilin 40Intrinsic isomerase activityNMR difference spectroscopySuccinyl-AlaExpression vectorHistidine residuesEscherichia coliTryptophan residuesProteinCyclophilinMolecular modellingAla-ProResiduesGel filtrationWeak affinityBindingHigh affinityAffinity matrix