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

Christian U. Lenzen, Diana Steinmann, Sidney W. Whiteheart, William I. Weis

Research output: Contribution to journalArticlepeer-review

290 Scopus citations


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 Å 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 δ' of E. coli DNA polymerase III. The structure suggests several regions responsible for coupling of ATP hydrolysis to structural changes in full-length NSF.

Original languageEnglish
Pages (from-to)525-536
Number of pages12
Issue number4
StatePublished - Aug 21 1998

Bibliographical note

Funding Information:
We thank D. Herschlag, A. Kolatkar, J. Kuriyan, E. Matveeva, K. Misura, and J. Wedekind for advice and discussions. C. U. L. was supported by a Deutsche Forschungsgemeinschaft Postdoctoral Fellowship. This work was supported by the National Institutes of Health (S. W. W.), the Pew Scholars Program in the Biomedical Sciences, and a Stanford University/Howard Hughes Medical Institute Junior Faculty award (W. I. W.).

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology


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