1d2n
D2 DOMAIN OF N-ETHYLMALEIMIDE-SENSITIVE FUSION PROTEIND2 DOMAIN OF N-ETHYLMALEIMIDE-SENSITIVE FUSION PROTEIN
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedN-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. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein.,Lenzen CU, Steinmann D, Whiteheart SW, Weis WI Cell. 1998 Aug 21;94(4):525-36. PMID:9727495[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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