Structural basis for EROS binding to human phagocyte NADPH oxidase NOX2.

ABSTRACT: Essential for reactive oxygen species (EROS) protein is a recently identified molecular chaperone of NOX2 (gp91^phox), the catalytic subunit of phagocyte NADPH oxidase. Deficiency in EROS is a recently identified cause for chronic granulomatous disease, a genetic disorder with recurrent bacterial and fungal infections. Here, we report a cryo-EM structure of the EROS-NOX2-p22^phox heterotrimeric complex at an overall resolution of 3.56Å. EROS and p22^phox are situated on the opposite sides of NOX2, and there is no direct contact between them. EROS associates with NOX2 through two antiparallel transmembrane (TM) α-helices and multiple β-strands that form hydrogen bonds with the cytoplasmic domain of NOX2. EROS binding induces a 79° upward bend of TM2 and a 48° b

SUBMITTER: Liang S 

PROVIDER: S-EPMC11161758 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature