1999
Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡
Sachpatzidis A, Dealwis C, Lubetsky J, Liang P, Anderson K, Lolis E. Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡. Biochemistry 1999, 38: 12665-12674. PMID: 10504236, DOI: 10.1021/bi9907734.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayEnzyme InhibitorsHydrogen BondingModels, MolecularOrganophosphonatesTryptophan SynthaseConceptsTransition stateShort hydrogen bondsTryptophan synthaseHigh conformational flexibilityTetrahedral transition stateTransition state analogueMechanism of catalysisEnzyme-inhibitor complexStructure-based approachPhosphonate oxygenIndole-3-glycerol phosphateHydroxyl oxygenHydrogen bondsSulfur atomsActive siteC3 atomC2 atomCrystal structureConformational flexibilityCrystallographic studiesInhibitor bindingConformation changeAtomsNew herbicidesGlu-49
1990
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Lolis E, Petsko G. Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. Biochemistry 1990, 29: 6619-25. PMID: 2204418, DOI: 10.1021/bi00480a010.Peer-Reviewed Original ResearchConceptsHydrogen bondsSide chainsGlu-165Triosephosphate isomeraseLatter hydrogen bondTransition state analogueFinal R factorEnzyme-inhibitor complexSpectroscopic resultsActive siteConformational changesCrystallographic analysisLoop movesPhosphoglycolic acidIsomeraseUnbound formCatalysisR factorBondsEnzymeComplexesStructural termsAtomic modelBindingChainStructure of yeast triosephosphate isomerase at 1.9-A resolution.
Lolis E, Alber T, Davenport R, Rose D, Hartman F, Petsko G. Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 1990, 29: 6609-18. PMID: 2204417, DOI: 10.1021/bi00480a009.Peer-Reviewed Original ResearchConceptsHydrogen bonding interactionsYeast triosephosphate isomeraseActive site structureNon-hydrogen atomsWater moleculesActive siteActive site residuesDrug designGlu-165Triosephosphate isomeraseSite structureCatalytic baseCrystal contactsSite residuesR factorTIM structuresFlexible loopLys-12Polypeptide chainStructureSubunit interfaceCarboxylateMonomersHydroxylFirst time