First Glimpse of the Crystal Structure of YaeT’s POTRA Domains | Zendy

Rajeev Misra | Zendy

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First 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.

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