1994
Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.
Joseph-McCarthy D, Lolis E, Komives E, Petsko G. Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site. Biochemistry 1994, 33: 2815-23. PMID: 8130194, DOI: 10.1021/bi00176a010.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesCrystallizationCrystallography, X-RayDNA PrimersLigandsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPoint MutationProtein FoldingProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiaeTriose-Phosphate IsomeraseX-Ray DiffractionConceptsMutant enzymesSubstrate-binding loopActive-site LysLys-12Wild-type enzymeMet side chainsActive siteEnzyme-inhibitor complexThree-dimensional structureMutant structuresWild typeTriosephosphate isomeraseDianionic substrateEnzymeSame crystal formCrystal structureMET mutationsSide chainsIsomeraseSitesCrystal formsMutationsPhosphoglycolohydroxamateMethionine
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 time