PDBsum entry: 1ckr

Chaperone

PDB id: 1ckr

Contents

Protein chain

159 a.a. *

* Residue conservation analysis

PDB id:

1ckr

Name:

Chaperone

Title:

High resolution solution structure of the heat shock cognate-70 kd substrate binding domain obtained by multidimensional nmr techniques

Structure:

Heat shock substrate binding domain of hsc-70. Chain: a. Fragment: substrate binding domain. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

R.C.Morshauser,W.Hu,H.Wang,Y.Pang,G.C.Flynn,E.R.P.Zuiderweg

Key ref:

R.C.Morshauser et al. (1999). High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70. J Mol Biol, 289, 1387-1403. PubMed id: 10373374 DOI: 10.1006/jmbi.1999.2776

Date:

22-Apr-99 Release date: 30-Apr-99

Protein chain

P63018  (HSP7C_RAT) -  Heat shock cognate 71 kDa protein

Seq: 646 a.a.

Struc: 159 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: ATP binding (1 term)

DOI no: 10.1006/jmbi.1999.2776

J Mol Biol 289:1387-1403 (1999)

PubMed id: 10373374

High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.

R.C.Morshauser, W.Hu, H.Wang, Y.Pang, G.C.Flynn, E.R.Zuiderweg.

ABSTRACT

The three-dimensional structure for the substrate-binding domain of the mammalian chaperone protein Hsc70 of the 70 kDa heat shock class (HSP70) is presented. This domain includes residues 383-540 (18 kDa) and is necessary for the binding of the chaperone with substrate proteins and peptides. The high-resolution NMR solution structure is based on 4150 experimental distance constraints leading to an average root-mean-square precision of 0.38 A for the backbone atoms and 0.76 A for all atoms in the beta-sandwich sub-domain. The protein is observed to bind residue Leu539 in its hydrophobic substrate-binding groove by intramolecular interaction. The position of a helical latch differs dramatically from what is observed in the crystal and solution structures of the homologous prokaryotic chaperone DnaK. In the Hsc70 structure, the helix lies in a hydrophobic groove and is anchored by a buried salt-bridge. Residues involved in this salt-bridge appear to be important for the allosteric functioning of the protein. A mechanism for interdomain allosteric modulation of substrate-binding is proposed. It involves large-scale movements of the helical domain, redefining the location of the hinge area that enables such motions.

Selected figure(s)

Figure 5.
Figure 5. The only hydrophobic residue in the C-terminal pseudo-substrate, Leu539, resides in a well-formed hydrophobic pocket.

Figure 6.
Figure 6. Bound Leu539 (green) lies in the center of a cluster of conserved hydrophobic residues. All contact residues are shown.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1999, 289, 1387-1403) copyright 1999.

Figures were selected by an automated process.