1bq0 | pdb_00001bq0
From Proteopedia
J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES
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Structural highlights
FunctionDNAJ_ECOLI Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.[1] [2] [3] [4] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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This page was last modified 15:35, 13 March 2024.