Literature summary for 2.1.1.297 extracted from

Holtkamp, W.; Kokic, G.; Jaeger, M.; Mittelstaet, J.; Komar, A.A.; Rodnina, M.V.
Cotranslational protein folding on the ribosome monitored in real time (2015), Science, 350, 1104-1107.

Search for more literature for 2.1.1.297

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of the crystal structure of the HemK N-terminal domain, PDB ID 1T43	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	mutated HemK N-terminal domain in which four conserved Leu residues occur, comprising the hydrophobic core of the N-terminal domain, are simultaneously replaced with Ala (4×A)	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ACC1	gene prmC	-

Synonyms

Synonyms	Comment	Organism
HemK	-	Escherichia coli
N5-glutamine methyltransferase	-	Escherichia coli
release factor glutamine methyltransferase	UniProt	Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
37	-	the isolated N-terminal domain with even a single Ala mutation is almost completely unfolded at 37°C	Escherichia coli

General Information

General Information	Comment	Organism
additional information	analysis of folding of a small five-helix protein domain at the N-terminal domain of Escherichia coli N5-glutamine methyltransferase HemK in real time. The isolated HemK N-terminal domain (residues 1 to 73) forms a stable alpha-helical structure independent of the C-terminal domain. Cotranslational folding of the protein, which folds autonomously and rapidly in solution, proceeds through a compact, non-native conformation that forms within the peptide tunnel of the ribosome. The compact state rearranges into a native-like structure immediately after the full domain sequence has emerged from the ribosome. Both folding transitions are rate-limited by translation, allowing for quasi-equilibrium sampling of the conformational space restricted by the ribosome. Cotranslational folding may be typical of small, intrinsically rapidly folding protein domains	Escherichia coli

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Release 2023.1 (January 2023)