| Autor: |
Jackson, M. E., Pratt, J. M. |
| Předmět: |
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| Zdroj: |
Molecular Microbiology; Sep1988, Vol. 2 Issue 5, p563-568, 6p |
| Abstrakt: |
Internal deletions close to the C-terminus of the Escherichia coli penicillin binding protein 5 (PBP5, DacA] have defined the C-terminal 18 residues of the protein as essential for membrane binding. This C-terminal sequence is capable of forming a strongly amphiphilic α-helix. In this paper we show that the PBP5 amphiphilic helix is able to anchor the periplasmic TEM-β-lactamase to the inner membrane. In addition, we have demonstrated that mature PBP5 (lacking the N-terminal signal sequence) possesses the ability to bind to the membrane from a soluble form of the protein, showing that translocation across the membrane is unnecessary for anchoring to be established. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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