Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.
N-ethylmaleimide-sensitive fusion protein (NSF) is a cytosolic ATPase required for many intracellular vesicle fusion reactions. NSF consists of an amino-terminal region that interacts with other components of the vesicle trafficking machinery, followed by two homologous ATP-binding cassettes, designated D1 and D2, that possess essential ATPase and hexamerization activities, respectively. The crystal structure of D2 bound to Mg2+-AMPPNP has been determined at 1.75 A resolution. The structure consists of a nucleotide-binding and a helical domain, and it is unexpectedly similar to the first two domains of the clamp-loading subunit delta' of E. coli DNA polymerase III. The structure suggests several regions responsible for coupling of ATP hydrolysis to structural changes in full-length NSF.
Lenzen
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Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.
Steinmann
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Whiteheart
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Weis
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D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics; D000266:Adenylyl Imidodiphosphate / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D003461:Crystallography; D004258:DNA Polymerase III / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D052066:N-Ethylmaleimide-Sensitive Proteins; D009711:Nucleotides / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D009711:Nucleotides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D033921:Vesicular Transport Proteins; D000266:Adenylyl Imidodiphosphate; D004258:DNA Polymerase III; D000251:Adenosine Triphosphatases; D052066:N-Ethylmaleimide-Sensitive Proteins