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

291 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.).

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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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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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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JO - Cell

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

Abstract

Bibliographical note

ASJC Scopus subject areas

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