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

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

doi:10.1016/S0092-8674(00)81593-7

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 journal › Article › peer-review

294 Scopus citations

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 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 language	English
Pages (from-to)	525-536
Number of pages	12
Journal	Cell
Volume	94
Issue number	4
DOIs	https://doi.org/10.1016/S0092-8674(00)81593-7
State	Published - 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.).

Funding

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.).

Funders	Funder number
Stanford University/Howard Hughes Medical Institute
National Institutes of Health (NIH)
Deutsche Forschungsgemeinschaft

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/S0092-8674(00)81593-7

Cite this

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title = "Crystal structure of the hexamerization domain of N-ethylmaleimide- sensitive fusion protein",

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 {\AA} 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.",

author = "Lenzen, \{Christian U.\} and Diana Steinmann and Whiteheart, \{Sidney W.\} and Weis, \{William I.\}",

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.). ",

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T1 - Crystal structure of the hexamerization domain of N-ethylmaleimide- sensitive fusion protein

AU - Lenzen, Christian U.

AU - Steinmann, Diana

AU - Whiteheart, Sidney W.

AU - Weis, William I.

N1 - 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.).

PY - 1998/8/21

Y1 - 1998/8/21

N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

Funding

ASJC Scopus subject areas

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