The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function

Structure. 1999 Feb 15;7(2):R19-23. doi: 10.1016/S0969-2126(99)80015-X.

Abstract

The hexameric structure of the D2 ATP-binding module of N-ethylmaleimide-sensitive factor (NSF), a chaperone involved in SNARE complex disassembly, was recently determined. This structure and the previously determined structure of the DNA polymerase III delta' subunit have far-reaching biological significance because these modules are related to diverse ATPases that promote the assembly, disassembly and operation of various protein complexes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Carrier Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Molecular Sequence Data
  • N-Ethylmaleimide-Sensitive Proteins
  • Protein Conformation
  • SNARE Proteins
  • Sequence Alignment
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Molecular Chaperones
  • SNARE Proteins
  • Vesicular Transport Proteins
  • Adenosine Triphosphate
  • N-Ethylmaleimide-Sensitive Proteins