Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein

Abstract

The cytosolic ATPase N-ethylmaleimide-sensitive fusion protein (NSF) disassembles complexes of membrane-bound proteins known as SNAREs, an activity essential for vesicular trafficking. The amino-terminal domain of NSF (NSF-N) is required for the interaction of NSF with the SNARE complex through the adaptor protein α-SNAP. The crystal structure of NSF-N reveals two subdomains linked by a single stretch of polypeptide. A polar interface between the two subdomains indicates that they can move with respect to one another during the catalytic cycle of NSF. Structure-based sequence alignments indicate that in addition to NSF orthologues, the p97 family of ATPases contain an amino-terminal domain of similar structure.

Cite this article

May, A., Misura, K., Whiteheart, S. et al. Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nat Cell Biol 1, 175–182 (1999). https://doi.org/10.1038/11097

View full text

>> Full Text:   Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein