1D2N

D2 DOMAIN OF N-ETHYLMALEIMIDE-SENSITIVE FUSION PROTEIN

Summary for 1D2N

• Entry DOI: 10.2210/pdb1d2n/pdb
• Descriptor: N-ETHYLMALEIMIDE-SENSITIVE FUSION PROTEIN, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: hexamerization domain, atpase, transport
• Biological source: Cricetulus griseus (Chinese hamster)
• Cellular location: Cytoplasm: P18708
• Total number of polymer chains: 1
• Total formula weight: 31160.20

Authors

Lenzen, C.U.,Steinmann, D.,Whiteheart, S.W.,Weis, W.I. (deposition date: 1998-06-30, release date: 1998-10-14, Last modification date: 2024-02-07)

Primary citation

Lenzen, C.U.,Steinmann, D.,Whiteheart, S.W.,Weis, W.I.
Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.
Cell(Cambridge,Mass.), 94:525-536, 1998

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.

PubMed: 9727495
DOI: 10.1016/S0092-8674(00)81593-7

Experimental method

X-RAY DIFFRACTION (1.75 Å)