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
2011
The crystal structure of GXGD membrane protease FlaK
Hu J, Xue Y, Lee S, Ha Y. The crystal structure of GXGD membrane protease FlaK. Nature 2011, 475: 528-531. PMID: 21765428, PMCID: PMC3894692, DOI: 10.1038/nature10218.Peer-Reviewed Original ResearchConceptsFamily of proteasesFirst crystal structureIntramembrane proteasesPrepilin peptidaseMethanococcus maripaludisMembrane proteasePreflagellin peptidaseFamilial Alzheimer's diseaseVirulence factorsAspartyl proteaseBiochemical analysisProteasePathogenic bacteriaStructural knowledgePresenilinPeptidaseCrystal structureSoluble counterpartActive siteFamilyRational designAspartylBacteriaAlzheimer's diseaseFundamental differences
2007
Open-cap conformation of intramembrane protease GlpG
Wang Y, Ha Y. Open-cap conformation of intramembrane protease GlpG. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 2098-2102. PMID: 17277078, PMCID: PMC1892946, DOI: 10.1073/pnas.0611080104.Peer-Reviewed Original ResearchConceptsIntramembrane proteasesEscherichia coli GlpGHydrophilic active sitePutative oxyanion holeActive siteMain-chain amidesPrevious crystallographic analysisRhomboid familyConformational plasticitySer-201Substrate bindingLoop L5GlpGClosed conformationSide portalsOpen conformationHydrophobic side chainsLoop movementOxyanion holeSide chainsPeptide bond hydrolysisLipid bilayersBond hydrolysisProteaseConformation
2006
Crystal structure of a rhomboid family intramembrane protease
Wang Y, Zhang Y, Ha Y. Crystal structure of a rhomboid family intramembrane protease. Nature 2006, 444: 179-180. PMID: 17051161, DOI: 10.1038/nature05255.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsBinding SitesCatalysisCell MembraneCrystallizationCrystallography, X-RayDNA-Binding ProteinsEndopeptidasesEscherichia coliEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsMembrane ProteinsModels, MolecularProtein Structure, TertiarySubstrate SpecificityWaterConceptsMembrane proteinsEscherichia coli GlpGÅ resolution crystal structureSite-2 proteaseIntegral membrane proteinsPutative active siteResolution crystal structureHydrophilic active siteRhomboid proteasesIntramembrane proteasesIntramembrane proteolysisTransmembrane segmentsTransmembrane domainActive siteProtease familyMembrane bilayerProtein interiorCore domainGating mechanismGlpGΓ-secretaseHydrophobic environmentCrystal structureProteaseLoop structure