Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase.

ABSTRACT: Lipocalin type prostaglandin D synthase (L-PGDS) is a multifunctional protein acting as a somnogen (PGD2)-producing enzyme, an extracellular transporter of various lipophilic ligands, and an amyloid-beta chaperone in human cerebrospinal fluid. In this study, we determined the crystal structures of two different conformers of mouse L-PGDS, one with an open cavity of the beta-barrel and the other with a closed cavity due to the movement of the flexible E-F loop. The upper compartment of the central large cavity contains the catalytically essential Cys65 residue and its network of hydrogen bonds with the polar residues Ser45, Thr67, and Ser81, whereas the lower compartment is composed of hydrophobic amino acid residues that are highly conserved among other lipocalins. SH titration analysis co

SUBMITTER: Kumasaka T 

PROVIDER: S-EPMC2755957 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature