Protein Family Models

PagL is an outer membrane protein with lipid A 3-O-deacylase activity. It forms an 8 stranded beta barrel structure [1]. [1]. 16632613. Crystal structure and catalytic mechanism of the LPS 3-O-deacylase PagL from Pseudomonas aeruginosa. Rutten L, Geurtsen J, Lambert W, Smolenaers JJ, Bonvin AM, de Haan A, van der Ley P, Egmond MR, Gros P, Tommassen J;. Proc Natl Acad Sci U S A. 2006;103:7071-7076. (from Pfam)

Date:

2024-10-16

PagL, as found in Salmonella enterica, is an embedded outer membrane protein that functions as a lipid A 3-O-deacylase. It belongs to Pfam family PF09411, a very diverse family including a distantly related lipid A 3-O-deacylase from Pseudomonas aeruginosa that also is called PagL.

Gene:

pagL

Date:

2021-07-23

acyloxyacyl hydrolase has lipid A 3-O-deacylase activity; it hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety

Date:

2017-10-04