PDBsum entry: 1fpo

Chaperone

PDB id: 1fpo

Contents

Protein chains

171 a.a. *

157 a.a. *

Waters ×449

* Residue conservation analysis

PDB id:

1fpo

Name:

Chaperone

Title:

Hsc20 (hscb), a j-type co-chaperone from e. Coli

Structure:

Chaperone protein hscb. Chain: a, b, c. Synonym: hsc20. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Hexamer (from PQS)

Resolution:

1.80Å R-factor: 0.216 R-free: 0.246

Authors:

J.R.Cupp-Vickery,L.E.Vickery

Key ref:

J.R.Cupp-Vickery and L.E.Vickery (2000). Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli. J Mol Biol, 304, 835-845. PubMed id: 11124030 DOI: 10.1006/jmbi.2000.4252

Date:

31-Aug-00 Release date: 08-Dec-00

Protein chains

P0A6L9  (HSCB_ECOLI) -  Co-chaperone protein hscB

Seq: 171 a.a.

Struc: 171 a.a.*

Protein chain

P0A6L9  (HSCB_ECOLI) -  Co-chaperone protein hscB

Seq: 171 a.a.

Struc: 157 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biological process: protein folding (1 term)
• Biochemical function: protein binding (3 terms)

DOI no: 10.1006/jmbi.2000.4252

J Mol Biol 304:835-845 (2000)

PubMed id: 11124030

Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.

J.R.Cupp-Vickery, L.E.Vickery.

ABSTRACT

Hsc20 is a 20 kDa J-protein that regulates the ATPase activity and peptide-binding specificity of Hsc66, an hsp70-class molecular chaperone. We report herein the crystal structure of Hsc20 from Escherichia coli determined to a resolution of 1.8 A using a combination of single isomorphous replacement (SIR) and multi-wavelength anomalous diffraction (MAD). The overall structure of Hsc20 consists of two distinct domains, an N-terminal J-domain containing residues 1-75 connected by a short loop to a C-terminal domain containing residues 84-171. The structure of the J-domain, involved in interactions with Hsc66, resembles the alpha-topology of J-domain fragments of Escherichia coli DnaJ and human Hdj1 previously determined by solution NMR methods. The C-terminal domain, implicated in binding and targeting proteins to Hsc66, consists of a three-helix bundle in which two helices comprise an anti-parallel coiled-coil. The two domains make contact through an extensive hydrophobic interface ( approximately 650 A(2)) suggesting that their relative orientations are fixed. Thus, Hsc20, in addition to its role in the regulation of the ATPase activity of Hsc66, may also function as a rigid scaffold to facilitate positioning of the protein substrates targeted to Hsc66.