Solution Structural Analysis of the Single-Domain Parvulin TbPin1 英文参考文献.docVIP

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Solution Structural Analysis of the Single-Domain Parvulin TbPin1 英文参考文献.doc

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Solution Structural Analysis of the Single-Domain Parvulin TbPin1 英文参考文献

SolutionStructuralAnalysisoftheSingle-Domain ParvulinTbPin1 LifangSun1,XuejiWu1,YuPeng2,JianYuanGoh3,Yih-CherngLiou3,4,DonghaiLin1*,YufenZhao1* 1The Key Laboratory of Chemical Biology of Fujian Province, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, China, 2NMR Laboratory, ShanghaiInstituteofMateriaMedica,ChineseAcademyofSciences,Shanghai,China,3NUSGraduateSchoolforIntegrativeSciencesandEngineering,NationalUniversity ofSingapore,Singapore,4DepartmentofBiologicalSciences,NationalUniversityofSingapore,Singapore Abstract Background:Pin1-typeparvulinsarephosphorylation-dependentpeptidyl-prolylcis-transisomerases.Theirfunctionshave beenwidelyreportedtobeinvolvedinavarietyofcellularresponsesorprocesses,suchascelldivision,transcription,and apoptosis,aswellasinhumandiseasesincludingAlzheimer’sdiseaseandcancers.TbPin1wasidentifiedasanovelclassof Pin1-typeparvulinsfromTrypanosomabrucei,containingauniquePPIasedomain,whichcancatalyzetheisomerizationof phosphorylatedSer/Thr-Propeptidebond. Methodology/Principal Findings: We determined the solution structure of TbPin1 and performed 15N relaxation measurementstoanalyzeitsbackbonedynamicsusingmulti-dimensionalheteronuclearNMRspectroscopy.Theaverage RMSDvaluesofthe20lowestenergystructuresare0.5060.05A? forbackboneheavyatomsand0.8560.08A? forallheavy atoms.TbPin1adoptsthetypicalcatalytictertiarystructureofPin1-typeparvulins,whichcomprisesaglobularfoldwitha four-strandedanti-parallelb-sheetcoresurroundedbythreea-helicesandone310-helix.TheglobalstructureofTbPin1is relativelyrigidexcepttheactivesite.The2DEXSYspectraillustratethatTbPin1possessesaphosphorylation-dependent PPIaseactivity.ThebindingsitesofTbPin1foraphosphorylatedpeptidesubstrate{SSYFSG[p]TPLEDDSD}weredetermined bythechemicalshiftperturbationapproach.ResiduesSer15,Arg18,Asn19,Val21,Ser22,Val32,Gly66,Ser67,Met83,Asp105 andGly107areinvolvedinsubstantialcontactwiththesubstrate. Conclusions/Significance:ThesolutionstructureofTbPin1andthebind