Open AccessMultiple mechanisms of membrane anchoring of Escherichia coli penicillin‐binding proteins
Author(s) -
Gittins John R.,
Phoenix David A.,
Pratt Julie M.
Publication year - 1994
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1111/j.1574-6976.1994.tb00031.x
Subject(s) - escherichia coli , penicillin binding proteins , biology , anchoring , bacterial outer membrane , microbiology and biotechnology , membrane protein , penicillin , escherichia coli proteins , biophysics , membrane , computational biology , biochemistry , antibiotics , gene , structural engineering , engineering
The major penicillin‐binding proteins (PBPs) of Escherichia coli play vital roles in cell wall biosynthesis and are located in the inner membrane. The high M r PBPs 1A, 1B, 2 and 3 are essential bifunctional transglycosylases/transpeptidases which are thought to be type II integral inner membrane proteins with their C‐terminal enzymatic domains projecting into the periplasm. The low M r PBP4 is a DD‐carboxypeptidase/endopeptidase, whereas PBPs 5 and are DD‐carboxypeptidases. All three low M r , PBPs act in the modification of peptidoglycan to allow expansion of the sacculus and are thought to be periplasmic proteins attached with varying affinities to the inner membrane via C‐terminal amphiphilic α‐helices. It is possible that the PBPs and other inner membrane proteins form a peptidoglycan synthesizing complex to coordinate their activities.