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

The cytosolic ATPase N-ethylmaleimide-sensitive fusion protein (NSF) disass embles complexes of membrane-bound proteins known as SNAREs, an activity es sential for vesicular trafficking. The aminoterminal domain of NSF (NSF-N) is required for the interaction of NSF with the SNARE complex through the a daptor protein alpha-SNAP. The crystal structure of NSF-N reveals two subdo mains 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 ind icate that in addition to NSF orthologues, the p97 family of ATPases contai n an amino-terminal domain of similar structure.