Structural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamily.

ABSTRACT: In this study we gain insight into the structural and functional characterization of the Aeropyrum pernix oligopeptide-binding protein (OppA(Ap)) previously identified from the extracellular medium of an Aeropyrum pernix cell culture at late stationary phase. OppA(Ap) showed an N-terminal Q32 in a pyroglutamate form and C-terminal processing at the level of a threonine-rich region probably involved in protein membrane anchoring. Moreover, the OppA(Ap) protein released into the medium was identified as a "nicked" form composed of two tightly associated fragments detachable only under strong denaturing conditions. The cleavage site E569-G570 seems be located on an exposed surface loop that is highly conserved in several three-dimensional (3D) structures of dipeptide/oligopeptide-binding prot

SUBMITTER: Balestrieri M 

PROVIDER: S-EPMC3021232 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature