Multiple mechanisms of membrane anchoring of Escherichia coli penicillin-binding proteins
Multiple mechanisms of membrane anchoring of Escherichia coli penicillin-binding proteins
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 Mr 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 Mr PBP4 is a DD-carboxypeptidase/endopeptidase, whereas PBPs 5 and are DD-carboxypeptidases. All three low Mr, 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 ?-helices. It is possible that the PBPs and other inner membrane proteins form a peptidoglycan synthesizing complex to coordinate their activities.
Penicillin-binding proteins, Escherichia coli, Membrane proteins, Anchoring mechanisms
1-12
Gittins, John R.
c4d269cc-aae0-4182-bc81-78dc724f7d95
Phoenix, David A.
04c27eae-3c4a-4dd2-bdbe-e7c32c7acd1b
Pratt, Julie M.
df3bb035-6890-4e20-8553-3dc65881c623
January 1994
Gittins, John R.
c4d269cc-aae0-4182-bc81-78dc724f7d95
Phoenix, David A.
04c27eae-3c4a-4dd2-bdbe-e7c32c7acd1b
Pratt, Julie M.
df3bb035-6890-4e20-8553-3dc65881c623
Gittins, John R., Phoenix, David A. and Pratt, Julie M.
(1994)
Multiple mechanisms of membrane anchoring of Escherichia coli penicillin-binding proteins.
FEMS Microbiology Reviews, 13 (1), .
(doi:10.1016/0168-6445(94)90097-3).
Abstract
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 Mr 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 Mr PBP4 is a DD-carboxypeptidase/endopeptidase, whereas PBPs 5 and are DD-carboxypeptidases. All three low Mr, 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 ?-helices. It is possible that the PBPs and other inner membrane proteins form a peptidoglycan synthesizing complex to coordinate their activities.
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Published date: January 1994
Keywords:
Penicillin-binding proteins, Escherichia coli, Membrane proteins, Anchoring mechanisms
Organisations:
Ocean and Earth Science
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Local EPrints ID: 380354
URI: http://eprints.soton.ac.uk/id/eprint/380354
ISSN: 0168-6445
PURE UUID: a8508f68-a431-438c-9cfc-ebc793dfb8b8
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Date deposited: 12 Aug 2015 16:18
Last modified: 14 Mar 2024 20:58
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Author:
David A. Phoenix
Author:
Julie M. Pratt
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