Mechanism of phage P22 tailspike protein folding mutations

@article{Danner1993MechanismOP,
  title={Mechanism of phage P22 tailspike protein folding mutations},
  author={Martina Danner and Robert Seckler},
  journal={Protein Science},
  year={1993},
  volume={2}
}
Temperature‐sensitive folding (tsf) and global‐tsf‐suppressor (su) point mutations affect the folding yields of the trimeric, thermostable phage P22 tailspike endorhamnosidase at elevated temperature, both in vivo and in vitro, but they have little effect on function and stability of the native folded protein. To delineate the mechanism by which these mutations modify the partitioning between productive folding and off‐pathway aggregation, the kinetics of refolding after dilution from acid‐urea… 
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TLDR
A shortened, recombinant protein comprising residues 109‐666 of the tailspike endorhamnosidase of Salmonella phage P22 was purified from Escherichia coli and crystallized and all six mutations were found to affect the thermal stability of the native protein.
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TLDR
The side-chain specificity at three tsf sites, together with structural examination in the tertiary fold, strongly suggests that destabilization of folding intermediates by loss of specific interactions is likely to be the major cause of the tsf defect in the dorsal fin domain.
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TLDR
The conception that the isolated beta-helix domain, although active in receptor-binding and native-like in its spectroscopic properties, is close in conformation to a crucial monomeric folding intermediate whose thermolability is responsible for the kinetic partitioning between productive folding and irreversible aggregation during the maturation process of P22 tailspike protein is conceived.
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TLDR
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  • Biology
    Journal of structural biology
  • 1998
TLDR
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A Concerted Mechanism for the Suppression of a Folding Defect through Interactions with Chaperones*
TLDR
The suppressor substitution likely improves folding in vivo through increased efficiency of coat protein-chaperone interactions.
Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike
TLDR
The impairment of tailspike maturation presumably reflects problems in the in vivo folding or assembly pathways, and the formation or reduction of the transient interchain disulfide bonds in the protrimer may be the locus of these kinetic functions.
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TLDR
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