Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP

@article{Yu1998StructureOT,
  title={Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP},
  author={Richard C. Yu and Phyllis I Hanson and Reinhard Jahn and Axel T. Br{\"u}nger},
  journal={Nature Structural Biology},
  year={1998},
  volume={5},
  pages={803-811}
}
N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase which primes and/or dissociates SNARE complexes involved in intracellular fusion events. Each NSF protomer contains three domains: an N-terminal domain required for SNARE binding and two ATPase domains, termed D1 and D2, with D2 being required for oligomerization. We have determined the 1.9 Å crystal structure of the D2 domain of NSF complexed with ATP using multi-wavelength anomalous dispersion phasing. D2 consists of a nucleotide… 
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References

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Each Domain of the N-Ethylmaleimide-sensitive Fusion Protein Contributes to Its Transport Activity (*)
TLDR
Data demonstrate that NSF binding to the SNAP•SNARE complex is mediated by the N domain and that both ATP binding and hydrolysis by the D1 domain are essential for 20 S particle dynamics.
N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
TLDR
It is demonstrated that the ability of the D1 domain to hydrolyze ATP is required for NSF activity and, therefore, required for membrane fusion.
N-Ethylmaleimide-sensitive Fusion Protein Contains High and Low Affinity ATP-binding Sites That Are Functionally Distinct*
TLDR
Nucleotide concentration greatly affected the ability of NSF to interact with α-SNAP·SNARE (soluble NSF attachment protein- SNAP receptor) complex, suggesting that only when the D1 domain ATP-binding sites are occupied does NSF bind to the α- SNPARE complex.
Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport.
TLDR
The idea that NSF incorporated into transport vesicles is nonexchangeable for exogenously added NSF is supported, as it was observed in wild-type NSF.
A Revised Model for the Oligomeric State of the N-Ethylmaleimide-sensitive Fusion Protein, NSF*
TLDR
The demonstration that NSF is a hexameric oligomer highlights structural similarities between it and several related ATPases which act by switching the conformational states of their protein substrates in order to activate them for subsequent reactions.
N-Ethylmaleimide-sensitive Factor Acts at a Prefusion ATP-dependent Step in Ca2+-activated Exocytosis*
TLDR
NSF-catalyzed activation of SNARE proteins may reorganize membranes to generate a vesicle-plasma membrane prefusion intermediate that is poised for conversion to full fusion by Ca2+-dependent mechanisms.
The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS
TLDR
The crystal structure of GroEL with ATPγS bound to each subunit shows that ATP binds to a novel pocket, whose primary sequence is highly conserved among chaperonins.
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