Probing the Putative Active Site of YjdL An Unusual Proton-Coupled Oligopeptide Transporter from E. coli 英文参考文献.docVIP

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Probing the Putative Active Site of YjdL An Unusual Proton-Coupled Oligopeptide Transporter from E. coli 英文参考文献.doc

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Probing the Putative Active Site of YjdL An Unusual Proton-Coupled Oligopeptide Transporter from E. coli 英文参考文献

ProbingthePutativeActiveSiteofYjdL:AnUnusual Proton-CoupledOligopeptideTransporterfromE.coli JohanneM?rchJensen1,FouziaIsmat2,GerdaSzakonyi3¤,MoazurRahman2,OsmanMirza1* 1Department ofDrugDesign andPharmacology, Facultyof Health andMedical Sciences, University ofCopenhagen, Copenhagen, Denmark, 2Health Biotechnology Division, NationalInstituteforBiotechnologyandGenetic Engineering,Faisalabad,Pakistan, 3Institute ofMembraneandSystemsBiology,UniversityofLeeds,Leeds, UnitedKingdom Abstract YjdL from E. coli is an unusual proton-coupled oligopeptide transporter (POT). Unlike prototypical POTs, dipeptides are preferredovertripeptides,inparticulardipeptideswithapositivelychargedC-terminalresidue.Tofurtherunderstandthis differenceinpeptidespecificity,thesequencesofYjdLandYdgR,aprototypicalE.coliPOT,werecomparedinlightofthe crystalstructureofaPOTfromShewanellaoneidensis.Severalresiduesfoundintheputativeactivesiteweremutatedand theactivitiesofthemutatedvariantswereassessedintermsofsubstrateuptakeassays,andchangesinspecificityinterms of uptake inhibition. Most strikingly, changing the YjdL specific Asp392 to the conserved Ser in YjdL obliterated the preference for a positively charged C-terminal residue. Based on this unique finding and previously published results indicatingthatthedipeptideN-terminusmayinteractwithGlu388,apreliminaryorientationmodelofadipeptideinthe YjdL cavity is presented. Single site mutations of particularly Ala281 and Trp278 support the presented orientation. A dipeptide bound in the cavity of YjdL appears to be oriented such that the N-terminal side chain protrudes into a sub pocket that opens towards the extracellular space. The C-terminal side chain faces in the opposite direction into a sub pocketthatfacesthecytoplasm.ThesedataindicatedastabilizingeffectonabulkyN-terminalresiduebyanAla281Phe variantandonthedipeptidebackbonebyTrp278.Inthepresentedorientationmodel,Tyr25andTyr58bothappeartobe in proximity of the dipeptide backbone while Lys117 appea