A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.

@article{Quigley2004ANN,
  title={A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.},
  author={Paulene M Quigley and Konstantin Korotkov and François Baneyx and Wim G. J. Hol},
  journal={Protein science : a publication of the Protein Society},
  year={2004},
  volume={13 1},
  pages={269-77}
}
Heat shock proteins and proteases play a crucial role in cell survival under conditions of environmental stress. The heat shock protein Hsp31, produced by gene hchA at elevated temperatures in Escherichia coli, is a homodimeric protein consisting of a large A domain and a smaller P domain connected by a linker. Two catalytic triads are present per dimer, with the Cys and His contributed by the A domain and an Asp by the P domain. A new crystal Form II confirms the dimer and catalytic triad… CONTINUE READING

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