1DG4 Chaperone date Nov 23, 1999
title Nmr Structure Of The Substrate Binding Domain Of Dnak In The Apo Form
authors M.Pellecchia, D.L.Montgomery, S.Y.Stevens, C.W.Van Der Kooi, H.Feng, L.M.Gierasch, E.R.P.Zuiderweg
compound source
Molecule: Dnak
Chain: A
Fragment: Substrate Binding Domain
Other_details: Molecular Chaperone
 Organism_scientific: Escherichia Coli
Organism_common: Bacteria
methodNMR, 20 Structures
similarity Belongs to the heat shock protein 70 family.[HSP70]
post-translat. modifications Autophosphorylated; grpe inhibits the autophosphorylation.
subcellular loc. Cytoplasmic; has also been isolated in association with the inner membrane.
genes dnaK, grpF, seg (E. coli)
function Also participates actively in the response to hyperosmotic shock. Plays an essential role in the initiation of phage lambda dna replication, where it acts in an atp-dependent fashion with the dnaj protein to release lambda o and p proteins from the preprimosomal complex. Dnak is also involved in chromosomal dna replication, possibly through an analogous interaction with the dnaa protein.
Gene
Ontology
ChainFunctionProcessComponent
A
  • nucleotide binding
  • ATP binding
  • unfolded protein binding
  • DNA replication
  • protein folding
  • response to unfolded protein...

    • Primary referenceStructural insights into substrate binding by the molecular chaperone DnaK., Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER, Nat Struct Biol 2000 Apr;7(4):298-303. PMID:10742174
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (542 Kb) [Save to disk]
  • Biological Unit Coordinates (1dg4.pdb1.gz) 552 Kb
  • CSU: Contacts of Structural Units for 1DG4
  • Retrieve 1DG4 in mmCIF format [Save to disk]
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        - Domain d1dg4a_, region A [Jmol] [rasmolscript] [script source]
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