1DG4 | Chaperone | date | Nov 23, 1999 | ||||||||
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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 | ||||||||||
method | NMR, 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 |
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Primary reference | Structural 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 |
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Visual 3D analysis of 1DG4 |
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Structure-derived information |
- Domain d1dg4a_, region A [Jmol] [rasmolscript] [script source] |
Sequence-derived information |
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