PMID:12621151
| Citation |
Quigley, PM, Korotkov, K, Baneyx, F and Hol, WG (2003) The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad. Proc. Natl. Acad. Sci. U.S.A. 100:3137-42 |
|---|---|
| Abstract |
Heat shock proteins (Hsps) play essential protective roles under stress conditions by preventing the formation of protein aggregates and degrading misfolded proteins. EcHsp31, the yedU (hchA) gene product, is a representative member of a family of chaperones that alleviates protein misfolding by interacting with early unfolding intermediates. The 1.6-A crystal structure of the EcHsp31 dimer reveals a system of hydrophobic patches, canyons, and grooves, which may stabilize partially unfolded substrate. The presence of a well conserved, yet buried, triad in each two-domain subunit suggests a still unproven hydrolytic function of the protein. A flexible extended linker between the A and P domains may play a role in conformational flexibility and substrate binding. The alpha-beta sandwich of the EcHsp31 monomer shows structural similarity to PhPI, a protease belonging to the DJ-1 superfamily. The structure-guided sequence alignment indicates that Hsp31 homologs can be divided in three classes based on variations in the P domain that dramatically affect both oligomerization and catalytic triad formation. |
| Links |
PubMed PMC152259 Online version:10.1073/pnas.0530312100 |
| Keywords |
Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Dimerization; Endopeptidases/chemistry; Endopeptidases/genetics; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/genetics; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Sequence Data; Protein Conformation; Protein Structure, Quaternary; Protein Subunits; Pyrococcus/enzymology; Pyrococcus/genetics; Sequence Homology, Amino Acid; Static Electricity |
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