Unique structural and ligand binding properties of the <i>Staphylococcus aureus</i> serine hydrolase FphE.

ABSTRACT: Staphylococcus aureus is a human pathogen capable of forming biofilms that complicate treatment and facilitate chronic infections. A family of S. aureus serine hydrolases are important regulators of virulence and biofilm formation. Among these, FphE is highly specific to S. aureus and therefor a viable target for both imaging and therapy. Here, we present bioinformatic and structural evidence that FphE may be involved in aromatic compound metabolism. In addition, twelve distinct crystal forms reveal that FphE exists as a highly unusual but stable and flexible, cross-subunit homodimer, unique to the large alpha/beta hydrolase superfamily. Substrate engagement favors retention of the dimeric state, which is a more catalytically active form of the enzyme and small angle X

SUBMITTER: Jo J 

PROVIDER: S-EPMC12632446 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature