PMID:11124030
| Citation |
Cupp-Vickery, JR and Vickery, LE (2000) Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli. J. Mol. Biol. 304:835-45 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1006/jmbi.2000.4252 |
| Keywords |
Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Conserved Sequence/genetics; Crystallography, X-Ray; Cysteine/genetics; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli Proteins; HSP40 Heat-Shock Proteins; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Humans; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Alignment; Static Electricity; Structure-Activity Relationship; Substrate Specificity |
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