First glimpse of the crystal structure of YaeT's POTRA domains.
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 beta-barrel domain and a soluble polypeptide-transport-associated (POTRA) domain. The POTRA domain is critical for substrate recognition and perhaps substrate folding, while the beta-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.
Misra
Rajeev
R
School of Life Sciences, Arizona State University, Tempe, Arizona 85287, USA. rajeev.misra@asu.edu
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D003460:Crystallization; D029968:Escherichia coli Proteins / Q000737:chemistry*; D054731:PDZ Domains; D017434:Protein Structure, Tertiary; D021381:Protein Transport
D001425:Bacterial Outer Membrane Proteins; C503914:BamA protein, E coli; D029968:Escherichia coli Proteins