ATP-triggered molecular mechanics of the chaperonin GroEL

ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the Groel Chaperonin.

METHOD--FLEXIBLE FITTING REFINEMENT PROTOCOL--X-RAY

SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD -2003.(DEPOSITION ID: 10412).

50 MM TRIS-HCL PH 7.4, 50 MM KCL AND 10 MM MGCL2, 200 UM ATP

THE DATA WERE COLLECTED WITH LEGINON AT SCRIPPS

VITRIFIED WITH A VITROBOT AT 100 PERCENT HUMIDITY WITH 2-3 SECONDS BLOTTING TIME

ATPASE MUTANT, CHAINS A-G ARE IN THE RDOPEN ATP BOUND CONFORMATION. CHAINS H-N ARE IN THE RD5 ATP BOUND CONFORMATION

CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7

CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL

CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX

CRYSTAL STRUCTURE OF THE HEXA-SUBSTITUTED MUTANT OF THEMOLECULAR CHAPERONIN GROEL APICAL DOMAIN

SOLUTION STRUCTURE OF APO GROEL BY CRYO-ELECTRON MICROSCOPY

SOLUTION STRUCTURE OF GROES-ADP7-GROEL-ATP7 COMPLEX BY CRYO-EM

STRUCTURAL AND MECHANISTIC BASIS FOR ALLOSTERY IN THEBACTERIAL CHAPERONIN GROEL; SEE REMARK 400

GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191 - 345

GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 191-376, MUTANT WITH ALA 262 REPLACED WITH LEU AND ILE 267 REPLACED WITH MET

STRUCTURAL BASIS FOR GROEL-ASSISTED PROTEIN FOLDING FROMTHE CRYSTAL STRUCTURE OF (GROEL-KMGATP)14 AT 2.0 ARESOLUTION

GRO-EL FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 188 -379

DOMAIN MOTIONS IN GROEL UPON BINDING OF AN OLIGOPEPTIDE

CRYSTAL STRUCTURE OF GROEL14-GROES7-(ADP-ALFX)7

FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)

FITTED COORDINATES FOR GROEL-ADP7-GROES CRYO-EM COMPLEX (EMD-1181)

REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)- ATP7 CRYO-EM MAP (EMD 1047)

CRYSTAL STRUCTURE OF THE ALLOSTERIC-DEFECTIVE CHAPERONIN GROEL E434K MUTANT