1990
Structure 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 timeCrystallographic 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 modelBindingChain
1987
Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
Alber T, Davenport R, Giammona D, Lolis E, Petsko G, Ringe D. Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme? Cold Spring Harbor Symposia On Quantitative Biology 1987, 52: 603-13. PMID: 3331346, DOI: 10.1101/sqb.1987.052.01.069.Peer-Reviewed Original Research