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