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Cell. 1998 Aug 21;94(4):525-36.

Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.

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1
Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.

Erratum in

  • Cell 1998 Oct 16;95(2):following 289.

Abstract

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.

PMID:
9727495
[Indexed for MEDLINE]
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