Abstract
The Omp85/YaeT family of proteins, which are conserved from bacteria to human, catalyzes insertion and assembly of proteins in the outer membrane. The structure consists of a transmembrane β-barrel domain and a soluble polypeptide-transport-associated (POTRA) domain. The POTRA domain is critical for substrate recognition and perhaps substrate folding, while the β-barrel domain assists in membrane insertion. The resolution of the crystal structure of the POTRA domain of the Escherichia coli YaeT protein provides a possible molecular mechanism by which the diverse group of substrates is recognized. Knowledge gained from the crystal structure may also spur the development of a novel class of chemotherapeutic inhibitors.
Original language | English (US) |
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Pages (from-to) | 649-651 |
Number of pages | 3 |
Journal | ACS Chemical Biology |
Volume | 2 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2007 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine