NSF N-terminal domain crystal structure: models of NSF function

Mol Cell. 1999 Jul;4(1):97-107. doi: 10.1016/s1097-2765(00)80191-4.

Abstract

N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase essential for eukaryotic vesicle fusion. Along with SNAP proteins, it disassembles cis-SNARE complexes upon ATP hydrolysis, preparing SNAREs for trans complex formation. We have determined the crystal structure of the N-terminal domain of NSF (N) to 1.9 A resolution. N contains two subdomains which form a groove that is a likely SNAP interaction site. Unexpectedly, both N subdomains are structurally similar to domains in EF-Tu. Based on this similarity, we propose a model for a large conformational change in NSF that drives SNARE complex disassembly.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • CHO Cells
  • Carrier Proteins / chemistry*
  • Cricetinae
  • Crystallography, X-Ray
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • N-Ethylmaleimide-Sensitive Proteins
  • Peptide Elongation Factor Tu / chemistry
  • Protein Conformation
  • Protein Structure, Secondary
  • Proteins / chemistry
  • Recombinant Proteins
  • SNARE Proteins
  • Selenoproteins
  • Sequence Alignment
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins*

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Proteins
  • Recombinant Proteins
  • SNARE Proteins
  • Selenoproteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins
  • Adenosine Triphosphate
  • Peptide Elongation Factor Tu
  • N-Ethylmaleimide-Sensitive Proteins

Associated data

  • PDB/1QCS