1N57

Crystal Structure of Chaperone Hsp31

Summary for 1N57

• Entry DOI: 10.2210/pdb1n57/pdb
• Descriptor: Chaperone Hsp31, MAGNESIUM ION (3 entities in total)
• Functional Keywords: alpha-beta sandwich, chaperone
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P31658
• Total number of polymer chains: 1
• Total formula weight: 32697.02

Authors

Quigley, P.M.,Korotkov, K.,Baneyx, F.,Hol, W.G.J. (deposition date: 2002-11-04, release date: 2003-03-18, Last modification date: 2024-11-13)

Primary citation

Quigley, P.M.,Korotkov, K.,Baneyx, F.,Hol, W.G.J.
The 1.6A Crystal Structure of the Class of Chaperone Represented by Escherichia coli Hsp31 Reveals a Putative Catalytic Triad
Proc.Natl.Acad.Sci.USA, 100:3137-3142, 2003

PubMed 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.

PubMed: 12621151
DOI: 10.1073/pnas.0530312100

Experimental method

X-RAY DIFFRACTION (1.6 Å)