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

Andrew P. May; Kira M.S. Misura; Sidney W. Whiteheart; William I. Weis

doi:10.1038/11097

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

Andrew P. May, Kira M.S. Misura, Sidney W. Whiteheart, William I. Weis

Molecular and Cellular Biochemistry

Research output: Contribution to journal › Article › peer-review

84 Scopus citations

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.

Original language	English
Pages (from-to)	175-182
Number of pages	8
Journal	Nature Cell Biology
Volume	1
Issue number	3
DOIs	https://doi.org/10.1038/11097
State	Published - Jul 1999

Funding

Funders	Funder number
National Heart, Lung, and Blood Institute (NHLBI)	R01HL056652
National Heart, Lung, and Blood Institute (NHLBI)

ASJC Scopus subject areas

Cell Biology

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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.",

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AB - 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.

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

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