Shin Hwa Young, Kang Wonchull, Lee Sang Yoon, Yang Jin Kuk
Department of Chemistry, College of Natural Sciences, Soongsil University, Seoul 156-743, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):41-3. doi: 10.1107/S1744309109047691. Epub 2009 Dec 25.
p97/VCP is a multifunctional AAA(+)-family ATPase that is involved in diverse cellular processes. p97/VCP directly interacts with various adaptors for activity in different biochemical contexts. Among these adaptors are p47 and Fas-associated factor 1 (FAF1), which contain a common UBX domain through which they bind to the N domain of p97/VCP. In the ubiquitin-proteasome pathway, p97/VCP acts as a chaperone that presents client proteins to the proteasome for degradation, while FAF1 modulates the process by interacting with ubiquitinated client proteins and also with p97/VCP. In an effort to elucidate the structural details of the interaction between p97/VCP and FAF1, the p97/VCP N domain was crystallized in complex with the FAF1 UBX domain. X-ray data were collected to 2.60 A resolution and the crystals belonged to space group C222(1), with unit-cell parameters a = 58.24, b = 72.81, c = 132.93 A. The Matthews coefficient and solvent content were estimated to be 2.39 A(3) Da(-1) and 48.4%, respectively, assuming that the asymmetric unit contained p97/VCP N domain and FAF1 molecules in a 1:1 ratio, which was subsequently confirmed by molecular-replacement calculations.
p97/VCP是一种多功能的AAA(+)家族ATP酶，参与多种细胞过程。p97/VCP在不同的生化环境中直接与各种衔接蛋白相互作用以发挥活性。这些衔接蛋白包括p47和Fas相关因子1（FAF1），它们含有一个共同的UBX结构域，通过该结构域与p97/VCP的N结构域结合。在泛素-蛋白酶体途径中，p97/VCP作为伴侣蛋白，将底物蛋白呈递给蛋白酶体进行降解，而FAF1通过与泛素化的底物蛋白以及p97/VCP相互作用来调节这一过程。为了阐明p97/VCP与FAF1之间相互作用的结构细节，p97/VCP的N结构域与FAF1的UBX结构域形成复合物并结晶。收集到了分辨率为2.60 Å的X射线数据，晶体属于空间群C222(1)，晶胞参数a = 58.24、b = 72.81、c = 132.93 Å。假设不对称单元中p97/VCP的N结构域和FAF1分子的比例为1:1，马修斯系数和溶剂含量分别估计为2.39 ų Da⁻¹和48.4%，这随后通过分子置换计算得到了证实。
