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={924-924}
}
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… CONTINUE READING
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Crystal structure of the hexamerization domain of N - ethylmaleimide - sensitive fusion protein

  • C. U. Lenzen, D. Oppitz, S. W. Whiteheart, W. I. Weis
  • 1998

Crystallography and NMR System ( CNS ) : A new software system for macromolecular structure determination . Acta Crystallogr . D , in the press (

  • A. T. Brünger
  • 1998

Improved structure refinement through maximum likelihood

  • N. S. Pannu, R. J. Read
  • Acta Crystallogr . A
  • 1996

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