Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein

Cell. 1998 Aug 21;94(4):525-36. doi: 10.1016/s0092-8674(00)81593-7.


N-ethylmaleimide-sensitive fusion protein (NSF) is a cytosolic ATPase required for many intracellular vesicle fusion reactions. NSF consists of an amino-terminal region that interacts with other components of the vesicle trafficking machinery, followed by two homologous ATP-binding cassettes, designated D1 and D2, that possess essential ATPase and hexamerization activities, respectively. The crystal structure of D2 bound to Mg2+-AMPPNP has been determined at 1.75 A resolution. The structure consists of a nucleotide-binding and a helical domain, and it is unexpectedly similar to the first two domains of the clamp-loading subunit delta' of E. coli DNA polymerase III. The structure suggests several regions responsible for coupling of ATP hydrolysis to structural changes in full-length NSF.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphatases / genetics
  • Adenylyl Imidodiphosphate / chemistry*
  • Amino Acid Sequence
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Crystallography
  • DNA Polymerase III / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • N-Ethylmaleimide-Sensitive Proteins
  • Nucleotides / metabolism
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid
  • Vesicular Transport Proteins*


  • Carrier Proteins
  • Nucleotides
  • Peptide Fragments
  • Recombinant Proteins
  • Vesicular Transport Proteins
  • Adenylyl Imidodiphosphate
  • DNA Polymerase III
  • Adenosine Triphosphatases
  • N-Ethylmaleimide-Sensitive Proteins

Associated data

  • PDB/1D2N