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

Research paper by A P AP May, K M KM Misura, S W SW Whiteheart, W I WI Weis

Indexed on: 13 Nov '99Published on: 13 Nov '99Published in: Nature Cell Biology


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 alpha-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.