Literature summary for 5.1.3.37 extracted from

Aachmann, F.L.; Svanem, B.I.; Guentert, P.; Petersen, S.B.; Valla, S.; Wimmer, R.
NMR structure of the R-module: a parallel beta-roll subunit from an Azotobacter vinelandii mannuronan C-5 epimerase (2006), J. Biol. Chem., 281, 7350-7356.

Crystallization (Commentary)

Crystallization (Comment)	Organism
NMR structure of the R-module from AlgE4. The R-module folds into a right-handed parallel beta-roll. Its overall shape is an elongated molecule with a positively charged patch that interacts with the substrate. Titration of the R-module with thulium indicates possible calcium binding sites in the loops formed by the nonarepeat sequences in the N-terminal part of the molecule. Calcium binding is important for the stability of the R-module. Calcium ions can be incorporated in these loops without structural violations and changes	Azotobacter vinelandii

Crystallization (Comment)

Organism

NMR structure of the R-module from AlgE4. The R-module folds into a right-handed parallel beta-roll. Its overall shape is an elongated molecule with a positively charged patch that interacts with the substrate. Titration of the R-module with thulium indicates possible calcium binding sites in the loops formed by the nonarepeat sequences in the N-terminal part of the molecule. Calcium binding is important for the stability of the R-module. Calcium ions can be incorporated in these loops without structural violations and changes

Azotobacter vinelandii

Organism

Organism	UniProt	Comment	Textmining
Azotobacter vinelandii	Q44493	-	-

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Release 2023.1 (January 2023)