Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells.
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Original identification and periplasmic localization of Spy.
"It encodes a precursor of a so far unknown 139-residue, rather basic periplasmic protein."
The crystal structure Escherichia coli Spy.
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.
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Establishes Spy as an ATP-independent aggregation-suppressing and refolding chaperone.
"In vitro studies demonstrate that the Spy protein is an effective ATP-independent chaperone that suppresses protein aggregation and aids protein refolding."
Super Spy variants implicate flexibility in chaperone action.
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Activity-enhanced variants link conformational flexibility to Spy chaperone performance.
"Our optimized Spy variants bind the client protein Im7 more tightly than wild type Spy does but are generally less stable suggesting that flexibility is important in the function of Spy as a chaperone."
Substrate protein folds while it is bound to the ATP-independent chaperone Spy.
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Quantitative binding and kinetic analysis demonstrates folding while continuously Spy-associated.
"A good fit was only achieved when we globally fit the data to the kinetic mechanism that allows both folding steps 4 and 5, i.e., complete folding of Im7 while bound to Spy"
Visualizing chaperone-assisted protein folding.
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Structural ensemble visualizes client progression across its folding landscape while bound to Spy.
"The ensemble shows that Spy-associated Im7 samples conformations ranging from unfolded to partially folded to native-like states and reveals how a substrate can explore its folding landscape while being bound to a chaperone."
UniProtKB entry for Escherichia coli Spy (P77754)
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Reviewed record summarizes ATP-independent aggregation suppression, refolding assistance, substrate-bound folding, and periplasmic localization.
"An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding."
Deep research report for Escherichia coli Spy
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Synthesizes Spy's periplasmic localization, aggregation suppression, refolding assistance, dimer architecture, and envelope-stress regulation.
Unfolded protein binding annotation review project