Protein Conformational Changes in the Bacteriorhodopsin Photocycle Comparison of Findings from Electron and X-Ray Crystallographic Analyses 英文参考文献.docVIP

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Protein Conformational Changes in the Bacteriorhodopsin Photocycle Comparison of Findings from Electron and X-Ray Crystallographic Analyses 英文参考文献.doc

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Protein Conformational Changes in the Bacteriorhodopsin Photocycle Comparison of Findings from Electron and X-Ray Crystallographic Analyses 英文参考文献

ProteinConformationalChangesinthe BacteriorhodopsinPhotocycle:ComparisonofFindings fromElectronandX-RayCrystallographicAnalyses TeruhisaHirai¤*,SriramSubramaniam* LaboratoryofCellBiology,NationalCancerInstitute,NationalInstitutesofHealth,Bethesda,Maryland,UnitedStatesofAmerica Abstract Light-drivenconformationalchangesinthemembraneproteinbacteriorhodopsinhavebeenstudiedextensivelyusingX- ray andelectron crystallography, resulting in the deposition of .30 sets of coordinates describing structural changes at various stages of proton transport. Using projection difference Fourier maps, we show that coordinates reported by different groups for the same photocycle intermediates vary considerably in the extent and nature of conformational changes.Thedifferentstructuresreportedforthesameintermediatecannotbereconciledintermsofdifferingextentsof changeonasingleconformationaltrajectory.Newmeasurementsofimagephasesobtainedbycryo-electronmicroscopyof the D96G/F171C/F219L triple mutant provide independent validation for the description of the large protein conformationalchangederivedat3.2A? resolutionbyelectroncrystallographyof2Dcrystals,butdonotsupportatomic modelsforlight-drivenconformationalchangesderivedusingX-raycrystallographyof3Dcrystals.Ourfindingssuggestthat independent determination of phase information from 2D crystals can be an important tool for testing the accuracy of atomicmodelsformembraneproteinconformationalchanges. Citation:HiraiT,SubramaniamS(2009)ProteinConformationalChangesintheBacteriorhodopsinPhotocycle:ComparisonofFindingsfromElectronandX-Ray CrystallographicAnalyses.PLoSONE4(6):e5769.doi:10.1371/journal.pone.0005769 Editor:JosephP.R.O.Orgel,IllinoisInstituteofTechnology,UnitedStatesofAmerica ReceivedDecember4,2008;AcceptedApril6,2009;PublishedJune2,2009 Thisisanopen-accessarticledistributedunderthetermsoftheCreativeCommonsPublicDomaindeclarationwhichstipulatesthat,onceplacedinthepublic domain,thisworkmaybefreelyreproduced,distributed,transmitted