1FPO

HSC20 (HSCB), A J-TYPE CO-CHAPERONE FROM E. COLI

Summary for 1FPO

• Entry DOI: 10.2210/pdb1fpo/pdb
• Descriptor: CHAPERONE PROTEIN HSCB (2 entities in total)
• Functional Keywords: molecular chaperone, chaperone
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 60503.08

Authors

Cupp-Vickery, J.R.,Vickery, L.E. (deposition date: 2000-08-31, release date: 2000-12-08, Last modification date: 2024-02-07)

Primary citation

Cupp-Vickery, J.R.,Vickery, L.E.
Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.
J.Mol.Biol., 304:835-845, 2000

PubMed 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.

PubMed: 11124030
DOI: 10.1006/jmbi.2000.4252

Experimental method

X-RAY DIFFRACTION (1.8 Å)