2.3.1.251	crystal structure of PagP in an SDS /2-methyl-2,4-pentanediol cosolvent system, to 1.4 A resolution. Phospholipid access occurs at the crenel present between strands F and G	
2.3.1.251	molecular dynamics simulation and comparison of Salmonella typhimurium and Escherichia coli enzymes. In vitro lipase activity of the Salmonella enzyme is 15-20fold higher than for the Escherichia coli enzyme. Protein stability correlates inversely with activity: the Escherichia coli PagP equilibrium free energy is 2fold higher	
2.3.1.251	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