Lenzen C U, Steinmann D, Whiteheart S W, Weis W I
Department of Structural Biology, Stanford University School of Medicine, California 94305, USA.
Cell. 1998 Aug 21;94(4):525-36. doi: 10.1016/s0092-8674(00)81593-7.
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.
N - 乙基马来酰亚胺敏感融合蛋白（NSF）是许多细胞内囊泡融合反应所需的一种胞质ATP酶。NSF由一个与囊泡运输机制的其他组分相互作用的氨基末端区域组成，随后是两个同源的ATP结合盒，分别命名为D1和D2，它们分别具有必需的ATP酶和六聚化活性。已在1.75埃分辨率下确定了与Mg2 + - AMPPNP结合的D2的晶体结构。该结构由一个核苷酸结合结构域和一个螺旋结构域组成，并且意外地类似于大肠杆菌DNA聚合酶III的钳位加载亚基δ'的前两个结构域。该结构表明了几个负责将ATP水解与全长NSF的结构变化偶联的区域。
