PMID:12642659
| Citation |
Wang, HW, Chen, Y, Yang, H, Chen, X, Duan, MX, Tai, PC and Sui, SF (2003) Ring-like pore structures of SecA: implication for bacterial protein-conducting channels. Proc. Natl. Acad. Sci. U.S.A. 100:4221-6 |
|---|---|
| Abstract |
SecA, an essential component of the general protein secretion pathway of bacteria, is present in Escherichia coli as soluble and membrane-integral forms. Here we show by electron microscopy that SecA assumes two characteristic forms in the presence of phospholipid monolayers: dumbbell-shaped elongated structures and ring-like pore structures. The ring-like pore structures with diameters of 8 nm and holes of 2 nm are found only in the presence of anionic phospholipids. These ring-like pore structures with larger 3- to 6-nm holes (without staining) were also observed by atomic force microscopic examination. They do not form in solution or in the presence of uncharged phosphatidylcholine. These ring-like phospholipid-induced pore-structures may form the core of bacterial protein-conducting channels through bacterial membranes. |
| Links |
PubMed PMC153074 Online version:10.1073/pnas.0737415100 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/ultrastructure; Bacterial Proteins; Escherichia coli/physiology; Escherichia coli/ultrastructure; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/ultrastructure; Ion Channels/chemistry; Liposomes; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/isolation & purification; Membrane Transport Proteins/ultrastructure; Microscopy, Atomic Force; Microscopy, Electron; Phospholipids/chemistry; Protein Conformation |
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