Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD.

@article{oldk2011CooperationOT,
  title={Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD.},
  author={Gabriel Žold{\'a}k and Franz Xaver Schmid},
  journal={Journal of molecular biology},
  year={2011},
  volume={406 1},
  pages={176-94}
}
The SlyD (sensitive to lysis D) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type. Here we investigated how the two domains and their interplay are optimized for function in protein folding. Unfolded protein molecules initially form a highly dynamic complex with the chaperone domain of SlyD, and they are then transferred to the prolyl isomerase domain. The turnover number of the prolyl isomerase site is very… CONTINUE READING

11 Figures & Tables

Connections & Topics

Mentioned Connections BETA
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Here we investigated how the two domains and their interplay are optimized for function in protein folding . Unfolded protein molecules initially form a highly dynamic complex with the chaperone domain of SlyD , and they
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Here we investigated how the two domains and their interplay are optimized for function in protein folding . Unfolded protein molecules initially form a highly dynamic complex with the chaperone domain of SlyD , and they
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Molecular ChaperonesGene product plays role in biological processprotein folding
Here we investigated how the two domains and their interplay are optimized for function in protein folding . Unfolded protein molecules initially form a highly dynamic complex with the chaperone domain of SlyD , and they
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD. The SlyD ( sensitive to lysis D ) protein of Escherichia coli is a folding enzyme with a chaperone domain and a prolyl isomerase domain of the FK506 binding protein type .
All Topics