Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA.

@article{Hunt2002NucleotideCO,
  title={Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA.},
  author={John Francis Hunt and Sevil Weinkauf and Lisa M Henry and John J. Fak and Paul M. McNicholas and Donald B. Oliver and Johann Deisenhofer},
  journal={Science},
  year={2002},
  volume={297 5589},
  pages={2018-26}
}
The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the… CONTINUE READING
Highly Influential
This paper has highly influenced a number of papers. REVIEW HIGHLY INFLUENTIAL CITATIONS

Connections & Topics

Mentioned Connections BETA
Adenosine TriphosphatasesIs biochemical function of gene productDNA Helicases
Comparisons with structurally related ATPases , including superfamily I and II ATP - dependent helicases , suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding , which is shown by fluorescence anisotropy experiments to reverse an endothermic domain - dissociation reaction hypothesized to gate binding to SecYEG .
Comparisons with structurally related ATPases , including superfamily I and II ATP - dependent helicases , suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding , which is shown by fluorescence anisotropy experiments to reverse an endothermic domain - dissociation reaction hypothesized to gate binding to SecYEG .
Comparisons with structurally related ATPases , including superfamily I and II ATP - dependent helicases , suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding , which is shown by fluorescence anisotropy experiments to reverse an endothermic domain - dissociation reaction hypothesized to gate binding to SecYEG .
Comparisons with structurally related ATPases , including superfamily I and II ATP - dependent helicases , suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding , which is shown by fluorescence anisotropy experiments to reverse an endothermic domain - dissociation reaction hypothesized to gate binding to SecYEG .
Comparisons with structurally related ATPases , including superfamily I and II ATP - dependent helicases , suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding , which is shown by fluorescence anisotropy experiments to reverse an endothermic domain - dissociation reaction hypothesized to gate binding to SecYEG .
All Topics