High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex

J Biol Chem. 2003 Mar 7;278(10):8630-6. doi: 10.1074/jbc.M211889200. Epub 2002 Dec 20.

Abstract

The structure of a truncated SNARE complex has been solved to 1.4-A resolution revealing a stabilizing salt bridge, sites of hydration, and conformational variability of the ionic central layer that were not observed in a previously published structure at 2.4-A resolution (Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. (1998) Nature 395, 347-353). The truncated complex lacks residues involved in phospholipid binding and denatures at a lower temperature than longer complexes as assessed by SDS and circular dichroism thermal melts. The truncated SNARE complex is monomeric, and it retains binding to synaptotagmin I.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biopolymers
  • Calcium-Binding Proteins*
  • Circular Dichroism
  • Crystallography, X-Ray
  • Membrane Glycoproteins / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Nerve Tissue Proteins / metabolism*
  • Neurons / metabolism*
  • Protein Binding
  • Protein Conformation
  • Rats
  • SNARE Proteins
  • Sequence Homology, Amino Acid
  • Synaptotagmin I
  • Synaptotagmins
  • Vesicular Transport Proteins*

Substances

  • Biopolymers
  • Calcium-Binding Proteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • SNARE Proteins
  • Synaptotagmin I
  • Syt1 protein, rat
  • Vesicular Transport Proteins
  • Synaptotagmins

Associated data

  • PDB/1N7S