1QCS

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

(1999) Mol Cell 4: 97-107

• PubMed: 10445031 Search on PubMed
• DOI: https://doi.org/10.1016/s1097-2765(00)80191-4
• Primary Citation of Related Structures:  
  1QCS


• PubMed 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.

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Organizational Affiliation: 

Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.