2020
Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation
Edani BH, Grabińska KA, Zhang R, Park EJ, Siciliano B, Surmacz L, Ha Y, Sessa WC. Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 20794-20802. PMID: 32817466, PMCID: PMC7456142, DOI: 10.1073/pnas.2008381117.Peer-Reviewed Original ResearchConceptsActive site tunnelProtein glycosylationAtomic resolution structuresGlycosyl carrier lipidsΑ3 helixEnzyme active sitePTase activityResolution structureActive siteEndoplasmic reticulumHomodimeric formCarrier lipidRate-limiting stepGlycosylationCrystal structureDHDDSStructural elucidationPTaseIsoprene chainPrenyltransferaseUnique insightsComplexesUnfavorable stateNgBRHomodimeric
2016
Mechanism of substrate specificity of phosphatidylinositol phosphate kinases
Muftuoglu Y, Xue Y, Gao X, Wu D, Ha Y. Mechanism of substrate specificity of phosphatidylinositol phosphate kinases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 8711-8716. PMID: 27439870, PMCID: PMC4978281, DOI: 10.1073/pnas.1522112113.Peer-Reviewed Original ResearchConceptsPhosphatidylinositol phosphate kinaseKinase familySubstrate specificityPhosphate kinasePhosphatidylinositol phosphate kinase (PIPK) familyZebrafish type IMembrane trafficking processesExquisite substrate specificityType III kinaseEukaryotic cellsInositol ringPhosphorylation resultsSubstrate recognitionTrafficking processesSpecificity loopPhosphatidylinositol derivativesBiological functionsPhosphatidylinositol 4PhosphatidylinositolKinaseStructural motifsType IBisphosphateLoop functionsComplex patterns