Falini Giuseppe, Fermani Simona, Tosi Giovanna, Arnesano Fabio, Natile Giovanni
Dipartimento di Chimica, G. Ciamician, Università di Bologna, via Selmi 2, 40126, Bologna, Italy.
Chem Commun (Camb). 2008 Dec 7(45):5960-2. doi: 10.1039/b813463d. Epub 2008 Oct 9.
A structural investigation performed on adducts of human ubiquitin with group-12 metal ions reveals common preferential anchoring sites, the most populated one being His68; at higher metal ion concentration a second and a third site, close to the N-terminus of the protein, become populated and promote a polymorphic transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the latter metal binding, undergo a remarkable displacement from their position in native ubiquitin; the aggregate stereochemistry appears to be driven by the clustering of deshielded backbone hydrogen-bond patches, and metal ions foster this process.
对人泛素与第12族金属离子加合物进行的结构研究揭示了常见的优先锚定位点，其中占据最多的是His68；在较高的金属离子浓度下，靠近蛋白质N端的第二个和第三个位点也被占据，并促进从正交晶型到立方晶型的多晶型转变；参与后一种金属结合的Glu16和Glu18相对于它们在天然泛素中的位置发生了显著位移；聚集体立体化学似乎是由去屏蔽的主链氢键斑块的聚集驱动的，金属离子促进了这一过程。
