NSF N-terminal domain crystal structure: models of NSF function.
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.
Yu
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Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.
Jahn
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Brunger
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D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002352:Carrier Proteins / Q000737:chemistry*; D006224:Cricetinae; D018360:Crystallography, X-Ray; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D052066:N-Ethylmaleimide-Sensitive Proteins; D010444:Peptide Elongation Factor Tu / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D011994:Recombinant Proteins; D050600:SNARE Proteins; D051140:Selenoproteins; D016415:Sequence Alignment; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D008565:Membrane Proteins; D011506:Proteins; D011994:Recombinant Proteins; D050600:SNARE Proteins; D051140:Selenoproteins; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D033921:Vesicular Transport Proteins; D000255:Adenosine Triphosphate; D010444:Peptide Elongation Factor Tu; D052066:N-Ethylmaleimide-Sensitive Proteins