Journal: Cellular and Molecular Life Sciences

Article Title: Hsp70 chaperones: Cellular functions and molecular mechanism

doi: 10.1007/s00018-004-4464-6

Figure Lengend Snippet: Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) ATPase domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b ) Compex of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).

Article Snippet: The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1.

Techniques: Derivative Assay, Binding Assay