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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.3 Methanocaldococcus jannaschii
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2.1.3.9 Methanocaldococcus jannaschii
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Synonyms

EC Number Synonyms Comment Organism
2.1.3.3 ornithine carbamoyltransferase
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 Methanocaldococcus jannaschii
2.1.3.3 otcase
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 Methanocaldococcus jannaschii
2.1.3.9 AOTCase
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 Methanocaldococcus jannaschii
2.1.3.9 MJ0366
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 Methanocaldococcus jannaschii
2.1.3.9 N-acetylornithine carbamoyltransferase
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 Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
2.1.3.3 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, EC 2.1.3.9, and an unknotted ornithine carbamoyltransferase, OTCase, 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
2.1.3.9 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