Abstract
N-ethylmaleimide-sensitive factor (NSF) is a hexameric ATPase essential for eukaryotic vesicle fusion. Along with SNAP proteins, it disassembles cis-SNARE complexes upon ATP hydrolysis, preparing SNAREs for trans complex formation. We have determined the crystal structure of the N-terminal domain of NSF (N) to 1.9 A resolution. N contains two subdomains which form a groove that is a likely SNAP interaction site. Unexpectedly, both N subdomains are structurally similar to domains in EF-Tu. Based on this similarity, we propose a model for a large conformational change in NSF that drives SNARE complex disassembly.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Animals
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CHO Cells
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Carrier Proteins / chemistry*
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Cricetinae
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Crystallography, X-Ray
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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 Elongation Factor Tu / chemistry
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Protein Conformation
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Protein Structure, Secondary
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Proteins / chemistry
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Recombinant Proteins
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SNARE Proteins
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Selenoproteins
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Sequence Alignment
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Membrane Proteins
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Proteins
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Recombinant Proteins
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SNARE Proteins
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Selenoproteins
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Vesicular Transport Proteins
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Adenosine Triphosphate
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Peptide Elongation Factor Tu
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N-Ethylmaleimide-Sensitive Proteins