Analysis of the membrane interactive potential of the escherichia coli pbp6b c-terminus

Title:Analysis of the membrane interactive potential of the escherichia coli pbp6b c-terminus

Volume: 7 Issue: 2

Author(s): David A. Phoenix*James Wallace

Affiliation:

• Department of Biological Sciences and 2Department of Physics, Astronomy and Mathematics, University of Central Lancashire, Preston, UK, PRI 2HE

Abstract: Escherichia coli low molecular weight penicillin binding proteins include PBP4,5,6 and recently PBP6b. PBP5 and PBP6 have been shown to possess C-terminal amphiphilic helical anchors. PBP4 has been shown to have the potential to interact at the membrane interface but the protein appears to bind via a different mechanism to PBP5 and PBP6. It has been suggested that since PBP6b has a high homology with PBP6 it also binds via an amphiphilic alpha helix. Here helical wheel, hydrophobic moment and DWIH analysis are used to show that the C-terminus of PBP6b does not resemble the anchor regions of the PBP5 and 6 but may stabilize membrane binding using a mechanism similar to that of PBP4.

Cite this article as:

Phoenix A. David*, Wallace James, Analysis of the membrane interactive potential of the escherichia coli pbp6b c-terminus, Protein & Peptide Letters 2000; 7 (2) . https://dx.doi.org/10.2174/092986650702221206114154

DOI https://dx.doi.org/10.2174/092986650702221206114154	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305