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 stepsAcidSitesShellSubstrateCrystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation
Lomakin IB, Dmitriev SE, Steitz TA. Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 116: 528-533. PMID: 30584092, PMCID: PMC6329987, DOI: 10.1073/pnas.1809688116.Peer-Reviewed Original ResearchConceptsTranslation initiationHeterodimer formationUnconventional translation initiationNoncanonical translation initiationZinc-binding siteMechanism of regulationUpstream reading framesIon-binding sitesRibosome recyclingReading frameTerminal domainTranslation reinitiationCysteine residuesAtomic detailHeterodimersMCT-1Crystal structureSpecific setReinitiationRibosomesProteinCysteineMRNAResiduesSites
2020
Crystal structure of the C-terminal domain of DENR
Lomakin IB, De S, Wang J, Borkar AN, Steitz TA. Crystal structure of the C-terminal domain of DENR. Computational And Structural Biotechnology Journal 2020, 18: 696-704. PMID: 32257053, PMCID: PMC7114459, DOI: 10.1016/j.csbj.2020.03.009.Peer-Reviewed Original ResearchNon-canonical translation initiationTerminal domainTranslation initiationRibosomal recyclingSequence homology modelingSmall ribosomal subunitInitiation factor eIF1N-terminal domainInitiation codon selectionMCT-1Low-resolution crystal structureIon-binding sitesStable heterodimerRibosomal subunitCodon selectionÅ resolutionSimilar foldHomology modelingHelix h44EIF1DENRRRNAP siteCrystal structureHeterodimers
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