Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.
The Uncharged Surface Features Surrounding the Active Site of Escherichia Coli Dsba are Conserved and are Implicated in Peptide Binding
Structural Analysis of Three His32 Mutants of Dsba: Support for an Electrostatic Role of His32 in Dsba Stability
Crystal Structure of the Dsba Protein Required for Disulphide Bond Formation in Vivo
Crystallization of Dsba, an Escherichia Coli Protein Required for Disulphide Bond Formation in Vivo
AQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHVNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKAAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYADTVKYLSEKK
27% PEG 4K IN 0.1M ACETATE BUFFER PH 5.0
EIGHT RESIDUES GLU 4, GLU 13, LYS 48, LYS 98, GLU 120, LYS 132, GLN 146, AND LYS 183 WERE MODELLED AS ALANINE BECAUSE OF POORLY DEFINED SIDE CHAIN DENSITY. RESIDUES GLU 85, SER 106, SER 133, AND SER 186 WERE MODELLED WITH TWO ALTERNATE CONFORMATIONS, EACH OF HALF OCCUPANCY. THE SIDE CHAINS OF GLU 13, GLU 85, SER 106, SER 133, AND SER 186 WERE MODELLED WITH TWO ALTERNATE CONFORMATIONS, EACH OF HALF OCCUPANCY.
OXIDOREDUCTASE, PROTEIN DISULFIDE ISOMERASE, PROTEIN FOLDING, REDOX PROTEIN, REDOX-ACTIVE CENTER
MKKIWLALAGLVLAFSASAAQYEDGKQYTTLEKPVAGAPQVLEFFSFFCPHCYQFEEVLHISDNVKKKLPEGVKMTKYHV NFMGGDLGKDLTQAWAVAMALGVEDKVTVPLFEGVQKTQTIRSASDIRDVFINAGIKGEEYDAAWNSFVVKSLVAQQEKA AADVQLRGVPAMFVNGKYQLNPQGMDTSNMDVFVQQYADTVKYLSEKK