1991
Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold.
Stallings W, Abdel-Meguid S, Lim L, Shieh H, Dayringer H, Leimgruber N, Stegeman R, Anderson K, Sikorski J, Padgette S, Kishore G. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 5046-5050. PMID: 11607190, PMCID: PMC51804, DOI: 10.1073/pnas.88.11.5046.Peer-Reviewed Original ResearchThree-dimensional structureSynthesis of aromatic amino acidsProtein-folding unitTwo-domain structureBinding of substratesPolypeptide backbone chainFour-stranded sheetFolding unitsGlobular domainSequence alterationsBeta-sheetEscherichia coliElectron density mapsBroad-spectrum herbicide glyphosateAromatic amino acidsApproximate dyadAmino acidsHelixProteinActive siteLinear sequenceEnzymeSequenceCrystallographic techniquesPseudo-symmetry
1988
Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements.
Anderson K, Sikorski J, Johnson K. Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements. Biochemistry 1988, 27: 1604-10. PMID: 3284585, DOI: 10.1021/bi00405a032.Peer-Reviewed Original ResearchConceptsBinding of substratesBinary complexShikimate 3-phosphateStopped-flow fluorescence methodsDissociation constantFree enzymeGlyphosate bindingS3P bindingInhibitor bindingProtein fluorescenceKinetics of bindingTernary complexEnzymeStopped-flowFluorescence measurementsBindingFluorescence titrationSaturating concentrationsS3PEquilibrium fluorescence measurements