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Escherichia coli BepA has proteolytic and chaperone‐like functions and acts in the degradation and biogenesis of β‐barrel outer membrane proteins (OMP). The tetratricopeptide repeat (TPR) domain of BepA (orange) interacts with proteins of the β‐barrel assembly machinery (BAM) complex (PDB code: 5D0O) as well as a substrate OMP (LptD; not shown), as visualized by in vivo photo‐cross‐linking. For details, see the article by Daimon et al . on pp. 760–776 of this issue.
Publication year - 2017
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13522
Subject(s) - tetratricopeptide , biology , biogenesis , bacterial outer membrane , chaperone (clinical) , escherichia coli , computational biology , biochemistry , microbiology and biotechnology , medicine , pathology , gene