Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein - PubMed (original) (raw)

Comparative Study

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

doi: 10.1016/s0092-8674(00)81593-7.

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• PMID: 9727495
• DOI: 10.1016/s0092-8674(00)81593-7

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Comparative Study

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

C U Lenzen et al. Cell. 1998.

Free article

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.

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