Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanocaldococcus jannaschii | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
AOTCase | - |
Methanocaldococcus jannaschii |
MJ0366 | - |
Methanocaldococcus jannaschii |
N-acetylornithine carbamoyltransferase | - |
Methanocaldococcus jannaschii |
General Information | Comment | Organism |
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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 |