Literature summary for 2.3.1.251 extracted from

Hwang, P.M.; Choy, W.Y.; Lo, E.I.; Chen, L.; Forman-Kay, J.D.; Raetz, C.R.; Prive, G.G.; Bishop, R.E.; Kay, L.E.
Solution structure and dynamics of the outer membrane enzyme PagP by NMR (2002), Proc. Natl. Acad. Sci. USA, 99, 13560-13565.

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Crystallization (Commentary)

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

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

Organism	UniProt	Comment	Textmining
Escherichia coli	P37001	-	-

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Release 2023.1 (January 2023)