Mycobacterium tuberculosis Glucosyl-3-Phosphoglycerate Synthase Structure of a Key Enzyme in Methylglucose Lipopolysaccharide Biosynthesis 英文参考文献.docVIP

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Mycobacterium tuberculosis Glucosyl-3-Phosphoglycerate Synthase Structure of a Key Enzyme in Methylglucose Lipopolysaccharide Biosynthesis 英文参考文献.doc

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Mycobacterium tuberculosis Glucosyl-3-Phosphoglycerate Synthase Structure of a Key Enzyme in Methylglucose Lipopolysaccharide Biosynthesis 英文参考文献

MycobacteriumtuberculosisGlucosyl-3- PhosphoglycerateSynthase:StructureofaKeyEnzyme inMethylglucoseLipopolysaccharideBiosynthesis PedroJose′ BarbosaPereira1,NunoEmpadinhas2,LucianaAlbuquerque2,BebianaSa′-Moura1,MiltonS. daCosta3,SandraMacedo-Ribeiro1* 1Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal, 2Centro de Neurocie?ncias e Biologia Celular, Departamento de Zoologia, UniversidadedeCoimbra,Coimbra,Portugal,3DepartamentodeBioqu?′mica,UniversidadedeCoimbra,Coimbra,Portugal Abstract Tuberculosis constitutes today a serious threat to human health worldwide, aggravated by the increasing number of identifiedmulti-resistantstrainsofMycobacteriumtuberculosis,itscausativeagent,aswellasbythelackofdevelopmentof novelmycobactericidalcompoundsforthelastfewdecades.Theincreasedresilienceofthispathogenisdue,toagreat extent,toitscomplex,polysaccharide-rich,andunusuallyimpermeablecellwall.Thesynthesisofthisessentialstructureis stillpoorlyunderstooddespitethefactthatenzymesinvolvedinglycosidicbondsynthesisrepresentmorethan1%ofallM. tuberculosisORFsidentifiedtodate.OneofthemisGpgS,aretainingglycosyltransferase(GT)withlowsequencehomology toanyotherGTsofknownstructure,whichhasbeenidentifiedintwospeciesofmycobacteriaandshowntobeessential forthesurvivalofM.tuberculosis.TofurtherunderstandthebiochemicalpropertiesofM.tuberculosisGpgS,wedetermined thethree-dimensionalstructureoftheapoenzyme,aswellasofitsternarycomplexwithUDPand3-phosphoglycerate,by X-raycrystallography,toaresolutionof2.5and2.7A,? respectively.GpgS,thefirstenzymefromthenewlyestablishedGT-81 familytobestructurallycharacterized,displaysadimericarchitecturewithanoverallfoldsimilartothatofotherGT-A-type glycosyltransferases.Thesethree-dimensionalstructuresprovideamolecularexplanationfortheenzyme’spreferencefor UDP-containing donor substrates, as well as for its glucose versus mannose discrimination, and uncover the structural determinants for acceptor substrate selectivity. Glycosy