Download MendeleyCrystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.
Lenzen, C.U., Steinmann, D., Whiteheart, S.W., Weis, W.I.(1998) Cell 94: 525-536
- PubMed: 9727495
- DOI: https://doi.org/10.1016/s0092-8674(00)81593-7
- Primary Citation of Related Structures:
1D2N - PubMed 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.
Organizational Affiliation:
Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.
