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 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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / drug effects
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Amino Acid Sequence
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Animals
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Carrier Proteins / chemistry*
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Carrier Proteins / drug effects
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Carrier Proteins / metabolism*
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Cloning, Molecular
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Cricetinae
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Cricetulus
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Crystallography, X-Ray / methods
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Ethylmaleimide / pharmacology*
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Humans
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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N-Ethylmaleimide-Sensitive Proteins
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Peptide Fragments / chemistry
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Protein Structure, Secondary
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Recombinant Proteins / chemistry
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Recombinant Proteins / drug effects
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Recombinant Proteins / metabolism
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SNARE Proteins
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Sequence Alignment
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Sequence Homology, Amino Acid
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Membrane Proteins
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Peptide Fragments
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Recombinant Proteins
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SNARE Proteins
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Vesicular Transport Proteins
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Adenosine Triphosphatases
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N-Ethylmaleimide-Sensitive Proteins
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Ethylmaleimide