Literature summary for 2.1.3.9 extracted from

Skrbic, T.; Micheletti, C.; Faccioli, P.
The role of non-native interactions in the folding of knotted proteins (2012), PLoS Comput. Biol., 8, e1002504.

Search for more literature for 2.1.3.9

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	-	-	-

Synonyms

Synonyms	Comment	Organism
AOTCase	-	Methanocaldococcus jannaschii
MJ0366	-	Methanocaldococcus jannaschii
N-acetylornithine carbamoyltransferase	-	Methanocaldococcus jannaschii

General Information

General Information	Comment	Organism
additional information	stochastic simulations of coarse-grained protein models used to investigate the propensity to form knots in early stages of protein folding, comparison of natively-knotted N-acetylornithine carbamoyltransferase, AOTCase, and an unknotted ornithine carbamoyltransferase, OTCase, EC 2.1.3.3, protein and amino acid interactions, mechanism, overview. The different entanglement of the two transcarbamylases follows from the tendency of the C-terminal to point away from (for OTCase) or approach and eventually thread (for AOTCase) other regions of partly-folded protein. The analysis of the OTCase/AOTCase pair clarifies that natively-knotted proteins can spontaneously knot during early folding stages and that non-native sequence-dependent interactions are important for promoting and disfavouring early knotting events. Knotting usually results from the threading of the C-terminal through loops present in the loose protein globule. Simulation of the early folding process of the two transcarbamylases, non-native interactions, kinetics, and modeling, overview	Methanocaldococcus jannaschii

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Release 2023.1 (January 2023)