2019-11-06RELPDBePDBePDBe2017-06-222017-08-162017-08-162019-11-06Wellcome Trust106252United KingdomWellcome Trust079605United KingdomWellcome Trust101488United KingdomMedical Research Council (United Kingdom)MR/M019292/1United KingdomBiotechnology and Biological Sciences Research CouncilBB/L014211/1United KingdomHartmut Hoffmann-Berling International Graduate School of Molecular and Cellular BiologyGermanyKnut and Alice Wallenberg Foundation and Family Erling Persson FoundationSwedenGerman Research FoundationMO 970/4-2GermanyGerman Research FoundationBB617/17-2GermanyCryo EM structure of the bacterial disaggregase ClpB (BAP form, DWB mutant), in the ATPgammaS state, bound to the model substrate caseinDeville CCarroni MFranke KBTopf MBukau BMogk ASaibil HRDeville CCarroni MFranke KBTopf MBukau BMogk ASaibil HRStructural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase.Sci AdvUS3e1701726e1701726201728798962doi:10.1126/sciadv.17017262375-2548EMD-3776associated EM volumeEMD-3777other EM volume5ofoFULLOVERLAPClpB homo hexamer bound to the model substract caseinClpB homo hexamer bound to the model substract casein012Escherichia coli0.57ClpB homo hexamer bound to the model substract casein11Escherichia coliClpB homo hexamer bound to the model substract casein12Bos taurusClpB (BAP form, double walker B mutant)Escherichia coliEscherichia coliLEVOMRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVSPLLTSAGINAGQLRTDINQALNRLPQVEGTGGDVQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDQLHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLEAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMMESEREKLLRMEQELHHRVIGQNEAVDAVSNAIRRSRAGLADPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDEAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDQVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGVRETERKSIGLIHQDNSTDAMEEIKKIFRPEFINRIDEVVVFHPLGEQHIASIAQIQLKRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNEDRIVAVQHAlpha caseinBos taurusLEVOMKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIG
SESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYK
VPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWY
YVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLWsingleParticleparticle0.77.425.0TrisHClTrisHCl25.0NaClsodium chloride10.0MgCl2magnesium chloride2.0ATPgS5'-O-(3-thio)triphosphate1.0DTTdithiothreitolLacey carbonCOPPER400CARBONLACEYGLOW DISCHARGEETHANE90295FEI VITROBOT MARK IIIblot force 0, blot time 3. FEI TITAN KRIOSFLOOD BEAMBRIGHT FIELDFIELD EMISSION GUN3002.71.03.5100000.FEI TITAN KRIOS AUTOGRID HOLDERNITROGENGIFGATAN K2 SUMMIT (4k x 4k)COUNTING1.01CTFFIND4C14.6FSC 0.143 CUT-OFFRELION2.0230000ANGULAR RECONSTITUTIONRELION2.0ANGULAR RECONSTITUTIONRELION2.0FLEXIBLE FITREALemd_3776_msk_1.mapemd_3776_half_map_1.map.gz1IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
256
256256
0
00256256256350.72350.72350.7290.090.090.0XYZ-0.0184747320.053292720.00025512650.00275593881.371.371.37emd_3776_half_map_2.map.gz1IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)