Structure and function of SecA, the preprotein translocase nanomotor
| Autor: | Eleftheria Vrontou, Anastassios Economou |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
SecA
Protein Conformation SecYEG Translocase of the outer membrane Bacterial Proteins Protein translocase Motor protein ATPase Translocase Molecular Biology Adenosine Triphosphatases Membrane transporter SecYEG Translocon SecA Proteins biology Membrane Transport Proteins Periplasmic space Cell Biology Cell biology Protein Transport Translocase of the inner membrane biology.protein Bacterial outer membrane Intermembrane space SEC Translocation Channels |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1694(1-3):67-80 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2004.06.003 |
| Popis: | Most secretory proteins that are destined for the periplasm or the outer membrane are exported through the bacterial plasma membrane by the Sec translocase. Translocase is a complex nanomachine that moves processively along its aminoacyl polymeric substrates effectively pumping them to the periplasmic space. The salient features of this process are: (a) a membrane-embedded “clamp” formed by the trimeric SecYEG protein, (b) a “motor” provided by the dimeric SecA ATPase, (c) regulatory subunits that optimize catalysis and (d) both chemical and electrochemical metabolic energy. Significant recent strides have allowed structural, biochemical and biophysical dissection of the export reaction. A model incorporating stepwise strokes of the translocase nanomachine at work is discussed. |
| Databáze: | OpenAIRE |
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