Neuwald A F
Cold Spring Harbor Laboratory, PO Box 1001, Bungtown Road, Cold Spring Harbor, NY 11724, USA.
Structure. 1999 Feb 15;7(2):R19-23. doi: 10.1016/S0969-2126(99)80015-X.
The hexameric structure of the D2 ATP-binding module of N-ethylmaleimide-sensitive factor (NSF), a chaperone involved in SNARE complex disassembly, was recently determined. This structure and the previously determined structure of the DNA polymerase III delta' subunit have far-reaching biological significance because these modules are related to diverse ATPases that promote the assembly, disassembly and operation of various protein complexes.
参与SNARE复合体拆解的分子伴侣N - 乙基马来酰亚胺敏感因子(NSF)的D2 ATP结合模块的六聚体结构最近已被确定。该结构以及先前确定的DNA聚合酶III δ'亚基的结构具有深远的生物学意义,因为这些模块与多种ATP酶相关,这些ATP酶促进各种蛋白质复合体的组装、拆解和运作。