Open AccessFirst Glimpse of the Crystal Structure of YaeT’s POTRA Domains
Author(s) -
Rajeev Misra
Publication year - 2007
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb700212p
Subject(s) - barrel (horology) , bacterial outer membrane , transmembrane protein , transmembrane domain , folding (dsp implementation) , domain (mathematical analysis) , biophysics , escherichia coli , substrate (aquarium) , membrane , biology , crystallography , chemistry , biochemistry , materials science , receptor , mathematical analysis , ecology , mathematics , electrical engineering , composite material , gene , engineering
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.