A Study on the C-Terminal Membrane Anchoring of Escherichia coli Penicillin-Binding Protein 5
Escherichia coli penicillin-binding protein 5 (PBP5) anchors to the inner membrane in a pH-dependent manner via a C-terminal amphiphilic α-helix. Low pH was found to enhance both levels of PBP5 membrane anchoring and levels of α-helicity in an aqueous PBP5 C-terminal homologue, which led to the sugg...
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Published in | Biochemical and biophysical research communications Vol. 290; no. 1; pp. 427 - 430 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
11.01.2002
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Subjects | |
Online Access | Get full text |
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Summary: | Escherichia coli penicillin-binding protein 5 (PBP5) anchors to the inner membrane in a pH-dependent manner via a C-terminal amphiphilic α-helix. Low pH was found to enhance both levels of PBP5 membrane anchoring and levels of α-helicity in an aqueous PBP5 C-terminal homologue, which led to the suggestion that levels of PBP5 membrane anchoring are related to levels of PBP5 C-terminal α-helicity. Here we have used Fourier-transformed infrared spectroscopy (FTIR) and a peptide homologue of the PBP5 C-terminal sequence to investigate the effect of pH on the conformational behavior of this sequence at a lipid interface and on its ability to interact with lipid. Our results suggest that the membrane-anchoring mechanism of PBP5 is unlikely to involve conformational change in the protein's C-terminal region and may therefore involve conformational changes in the protein's ectomembranous domain. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1006/bbrc.2001.6198 |