Crystallization (Comment) | Organism |
---|---|
solution NMR spectroscopy of PagP in both dodecylphosphocholine and n-octyl-beta-D-glucoside detergent micelles. PagP consists of an eight-stranded anti-parallel beta-barrel preceded by an amphipathic alpha-helix. The beta-barrel is well defined, whereas the loops connecting individual beta-strands show considerable mobility. Three amino acid residues critical for enzymatic activity localize to extracellular loops near the membrane interface. The active site of PagP is situated on the outer surface of the outer membrane | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P37001 | - |
- |