Featured Publications
The Crystal Structure of Yeast Fatty Acid Synthase, a Cellular Machine with Eight Active Sites Working Together
Lomakin IB, Xiong Y, Steitz TA. The Crystal Structure of Yeast Fatty Acid Synthase, a Cellular Machine with Eight Active Sites Working Together. Cell 2007, 129: 319-332. PMID: 17448991, DOI: 10.1016/j.cell.2007.03.013.Peer-Reviewed Original ResearchConceptsCatalytic siteCrystal structureAcyl carrier proteinPantetheine armActive siteCatalytic centerMacromolecular assembliesYeast fatty acid synthaseReaction chamberKetoacyl synthase domainWhole metabolic pathwaysTwo-dimensional diffusionAssemblyCarrier proteinSynthesisStructureComplexesCellular machinesMultiple stepsAcidSitesShellSubstrateThe joining of ribosomal subunits in eukaryotes requires eIF5B
Pestova T, Lomakin I, Lee J, Choi S, Dever T, Hellen C. The joining of ribosomal subunits in eukaryotes requires eIF5B. Nature 2000, 403: 332-335. PMID: 10659855, DOI: 10.1038/35002118.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCatalysisCodon, InitiatorEukaryotic Initiation Factor-1Eukaryotic Initiation Factor-2Eukaryotic Initiation Factor-3Eukaryotic Initiation Factor-5GTP PhosphohydrolasesGuanosine TriphosphateGuanylyl ImidodiphosphateHumansHydrolysisMolecular Sequence DataPeptide Chain Initiation, TranslationalPeptide Initiation FactorsPuromycinRecombinant ProteinsRibosomesRNA, MessengerConceptsEIF2-bound GTPEukaryotic initiation factor 3RNA ternary complexRibosome-dependent GTPase activityInitiation factor IF2Initiation factor 3Eukaryotic protein synthesisRibosomal subunitInitiation codonGTPase activityProtein synthesisMessenger RNASubunitsTernary complexFactor 3GTPComplexesEukaryotesEIF5EIF5BEIF2EIF4BEIF1ARibosomesIF2
2017
Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1
Lomakin IB, Stolboushkina EA, Vaidya AT, Zhao C, Garber MB, Dmitriev SE, Steitz TA. Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1. Cell Reports 2017, 20: 521-528. PMID: 28723557, PMCID: PMC5551485, DOI: 10.1016/j.celrep.2017.06.025.Peer-Reviewed Original ResearchConceptsSmall ribosomal subunitTranslation initiationRibosomal subunitUnconventional translation initiationInitiation factor 1Cancer-related mRNAsTranslational controlHuman ribosomeTerminal domainReinitiation stepsRibosomesDimer interactsFunctional implicationsFactor 1SubunitsCrystal structureStriking similaritySpecific setComplexesHeterodimersProteinOncoproteinInitiationInteractsMRNA