Article
The C terminus of SecA is involved in both lipid binding and SecB binding.
The Journal of biological chemistry - 7 Apr 1995
Breukink E, Nouwen N, van Raalte A, Mizushima S, Tommassen J, de Kruijff B
Abstract excerpt
Using C-terminal deletion mutations in secA, we localized the previously proposed (Breukink, E., Keller, R.C. A., and de Kruijff, B. (1993), FEBS Lett. 331, 19-24) second lipid binding site on SecA. Since removal of these residues completely abolished the property of SecA to cause aggregation of negatively charged phosphatidyl-glycerol vesicles, we conclude that the C-terminal 70 amino acid residues of SecA are...
Topics
- Adenosine Triphosphatases
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Biological Transport
- Escherichia coli Proteins
- Intracellular Membranes
- Lipid Metabolism
- Membrane Transport Proteins
- Molecular Sequence Data